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. 1982 Sep;46(3):308–340. doi: 10.1128/mr.46.3.308-340.1982

Comparative biochemistry of the proteinases of eucaryotic microorganisms.

M J North
PMCID: PMC281547  PMID: 6813664

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Selected References

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  1. ABOU AKKADA A. R., HOWARD B. H. The biochemistry of rumen protozoa. 5. The nitrogen metabolism of Entodinium. Biochem J. 1962 Feb;82:313–320. doi: 10.1042/bj0820313. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Abita J. P., Delaage M., Lazdunski M. The mechanism of activation of trypsinogen. The role of the four N-terminal aspartyl residues. Eur J Biochem. 1969 Apr;8(3):314–324. doi: 10.1111/j.1432-1033.1969.tb00530.x. [DOI] [PubMed] [Google Scholar]
  3. Achstetter T., Ehmann C., Wolf D. H. New proteolytic enzymes in yeast. Arch Biochem Biophys. 1981 Apr 1;207(2):445–454. doi: 10.1016/0003-9861(81)90052-7. [DOI] [PubMed] [Google Scholar]
  4. Allis C. D., Bowen J. K., Abraham G. N., Glover C. V., Gorovsky M. A. Proteolytic processing of histone H3 in chromatin: a physiologically regulated event in Tetrahymena micronuclei. Cell. 1980 May;20(1):55–64. doi: 10.1016/0092-8674(80)90234-2. [DOI] [PubMed] [Google Scholar]
  5. Asgari M., Henney H. R., Jr Inhibition of growth and cell wall morphogenesis of Bacillus subtilis by extracellular slime produced by Physarum flavicomum. Cytobios. 1977;20(79-80):163–177. [PubMed] [Google Scholar]
  6. Avila J. L., Casanova M. A., Avila A., Bretaña A. Acid and neutral hydrolases in Trypanosoma cruzi. Characterization and assay. J Protozool. 1979 May;26(2):304–311. doi: 10.1111/j.1550-7408.1979.tb02786.x. [DOI] [PubMed] [Google Scholar]
  7. Bai Y., Hayashi R. Properties of the single sulfhydryl group of carboxypeptidase Y. Effects of alkyl and aromatic mercurials on activities toward various synthetic substrates. J Biol Chem. 1979 Sep 10;254(17):8473–8479. [PubMed] [Google Scholar]
  8. Banyal H. S., Misra G. C., Gupta C. M., Dutta G. P. Involvement of malarial proteases in the interaction between the parasite and host erythrocyte in Plasmodium knowlesi infections. J Parasitol. 1981 Oct;67(5):623–626. [PubMed] [Google Scholar]
  9. Baranova N. A., Krykhtina N. M., Egorov N. S. Vliianie sostava sredy na sintez ékzoproteaz gribom Aspergillus candidus shtamm 70. Nauchnye Doki Vyss Shkoly Biol Nauki. 1979;(6):73–76. [PubMed] [Google Scholar]
  10. Barry F. P., Doonan S., Ross C. A. Cleavage by trypsin and by the proteinase from Armillaria mellea at epsilon-N-formyl-lysine residues. Biochem J. 1981 Mar 1;193(3):737–742. doi: 10.1042/bj1930737. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Beck I., Fink G. R., Wolf D. H. The intracellular proteinases and their inhibitors in yeast. A mutant with altered regulation of proteinase A inhibitor activity. J Biol Chem. 1980 May 25;255(10):4821–4828. [PubMed] [Google Scholar]
  12. Bertini F., Brandes D., Buetow D. E. Increased acid hydrolase activity during carbon starvation in Euglena gracilis. Biochim Biophys Acta. 1965 Aug 24;107(1):171–173. doi: 10.1016/0304-4165(65)90414-9. [DOI] [PubMed] [Google Scholar]
  13. Betz H. Loss of sporulation ability in a yeast mutant with low proteinase A levels. FEBS Lett. 1979 Apr 1;100(1):171–174. doi: 10.1016/0014-5793(79)81157-6. [DOI] [PubMed] [Google Scholar]
  14. Betz H., Weisner U. Protein degradation and proteinases during yeast sporulation. Eur J Biochem. 1976 Feb 2;62(1):65–76. doi: 10.1111/j.1432-1033.1976.tb10098.x. [DOI] [PubMed] [Google Scholar]
  15. Blum J. J. Effects of metabolites present during growth of Tetrahymena pyriformis on the subsequent secretion of lysosomal hydrolases. J Cell Physiol. 1975 Aug;86(1):131–142. doi: 10.1002/jcp.1040860115. [DOI] [PubMed] [Google Scholar]
  16. Blum J. J. Lysosomal hydrolase secretion by Tetrahymena: a comparison of several intralysosomal enzymes with the isoenzymes released into the medium. J Cell Physiol. 1976 Nov;89(3):457–472. doi: 10.1002/jcp.1040890311. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Bongertz V., Hungerer K. D. Trypanosoma cruzi: isolation and characterization of a protease. Exp Parasitol. 1978 Jun;45(1):8–18. doi: 10.1016/0014-4894(78)90039-5. [DOI] [PubMed] [Google Scholar]
  18. Bosmann H. B. Protein catabolism. II. Identification of neutral and acidic proteolytic enzymes in Aspergillus niger. Biochim Biophys Acta. 1973 Feb 15;293(2):476–489. doi: 10.1016/0005-2744(73)90354-9. [DOI] [PubMed] [Google Scholar]
  19. Braun P. C., Calderone R. A. Regulation and solubilization of Candida albicans chitin synthetase. J Bacteriol. 1979 Nov;140(2):666–670. doi: 10.1128/jb.140.2.666-670.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Braun V., Hantke K., Wolff H., Gerisch G. Degradation of the murein-lipoprotein complex of Escherichia coli cell walls by Dictyostelium amoebae. Eur J Biochem. 1972 May;27(1):116–125. doi: 10.1111/j.1432-1033.1972.tb01817.x. [DOI] [PubMed] [Google Scholar]
  21. Bromberg S. K., Schwalb M. N. Sporulation in Schizophyllum commune: changes in enzyme activity. Mycologia. 1978 May-Jun;70(3):481–486. [PubMed] [Google Scholar]
  22. COOK L., GRANT P. T., KERMACK W. O. Proteolytic enzymes of the erythrocytic forms of roden and simian species of malarial plasmodia. Exp Parasitol. 1961 Nov;11:372–379. doi: 10.1016/0014-4894(61)90041-8. [DOI] [PubMed] [Google Scholar]
  23. Camargo E. P., Itow S., Alfieri S. C. Proteolytic activities in cell extracts of trypanosomatids. J Parasitol. 1978 Dec;64(6):1120–1121. [PubMed] [Google Scholar]
  24. Chan V. L., Lee P. Y. Host-cell specific proteolytic enzymes in Plasmodium berghei infected erythrocytes. Southeast Asian J Trop Med Public Health. 1974 Sep;5(3):447–449. [PubMed] [Google Scholar]
  25. Chang W. J., Horiuchi S., Takahashi K., Yamasaki M., Yamada Y. The structure and function of acid proteases. VI. Effects of acid protease-specific inhibitors on the acid proteases from Aspergillus niger var. macrosporus. J Biochem. 1976 Nov;80(5):975–981. doi: 10.1093/oxfordjournals.jbchem.a131385. [DOI] [PubMed] [Google Scholar]
  26. Charet P., Ruffin P., Dherin M., Dubremetz J. F., Bouquelet S. Aminopeptidase of Eimeria nieschulzi physico-chemical properties and action of antimalarial drugs. Ann Parasitol Hum Comp. 1980 Jul-Aug;55(4):359–366. doi: 10.1051/parasite/1980554359. [DOI] [PubMed] [Google Scholar]
  27. Ciejek E., Thorner J. Recovery of S. cerevisiae a cells from G1 arrest by alpha factor pheromone requires endopeptidase action. Cell. 1979 Nov;18(3):623–635. doi: 10.1016/0092-8674(79)90117-x. [DOI] [PubMed] [Google Scholar]
  28. Cino P. M., Tewari R. P. Proteolytic activity of Oidiodendron kalrai. Can J Microbiol. 1975 Sep;21(9):1362–1368. doi: 10.1139/m75-204. [DOI] [PubMed] [Google Scholar]
  29. Cohen B. L., Drucker H. Regulation of exocellular protease in Neurospora crassa: induction and repression under conditions of nitrogen starvation. Arch Biochem Biophys. 1977 Aug;182(2):601–613. doi: 10.1016/0003-9861(77)90541-0. [DOI] [PubMed] [Google Scholar]
  30. Cohen B. L., Morris J. E., Drucker H. Regulation of two extracellular proteases of Neurospora crassa by induction and by carbon-nitrogen and sulfur-metabolite repression. Arch Biochem Biophys. 1975 Jul;169(1):324–330. doi: 10.1016/0003-9861(75)90347-1. [DOI] [PubMed] [Google Scholar]
  31. Cohen B. L. Regulation of intracellular and extracellular neutral and alkaline proteases in Aspergillus nidulans. J Gen Microbiol. 1973 Dec;79(2):311–320. doi: 10.1099/00221287-79-2-311. [DOI] [PubMed] [Google Scholar]
  32. Cohen B. L. The neutral and alkaline proteases of Aspergillus nidulans. J Gen Microbiol. 1973 Aug;77(2):521–528. doi: 10.1099/00221287-77-2-521. [DOI] [PubMed] [Google Scholar]
  33. Colotelo N. Fungal exudates. Can J Microbiol. 1978 Oct;24(10):1173–1181. doi: 10.1139/m78-191. [DOI] [PubMed] [Google Scholar]
  34. Cook R. T., Aikawa M., Rock R. C., Little W., Sprinz H. The isolation and fractionation of Plasmodium knowlesi. Mil Med. 1969 Sep;134(10):866–883. [PubMed] [Google Scholar]
  35. Coombs G. H. Proteinases of Leishmania mexicana and other flagellate protozoa. Parasitology. 1982 Feb;84(1):149–155. doi: 10.1017/s003118200005174x. [DOI] [PubMed] [Google Scholar]
  36. Cooper S., Chambers D. A., Scanlon S. Identification and characterization of the adenosine 3',5'-cyclic monophosphate binding proteins appearing during the development of Dictyostelium discoideum. Biochim Biophys Acta. 1980 May 7;629(2):235–242. doi: 10.1016/0304-4165(80)90097-5. [DOI] [PubMed] [Google Scholar]
  37. Correa J. U., Lemos E. M., Lodi W. R. Inhibition of sporulation in the water mold Blastocladiella emersonii by antipain. Dev Biol. 1978 Oct;66(2):470–479. doi: 10.1016/0012-1606(78)90252-x. [DOI] [PubMed] [Google Scholar]
  38. Côté C., Solioz M., Schatz G. Biogenesis of the cytochrome bc1 complex of yeast mitochondria. A precursor form of the cytoplasmically made subunit V. J Biol Chem. 1979 Mar 10;254(5):1437–1439. [PubMed] [Google Scholar]
  39. DICKIE N., LIENER I. E. A study of the proteolytic system of Tetrahymena pyriformis W. I. Purification and partial characterization of the constituent proteinases. Biochim Biophys Acta. 1962 Oct 8;64:41–51. doi: 10.1016/0006-3002(62)90758-8. [DOI] [PubMed] [Google Scholar]
  40. DICKIE N., LIENER I. E. A study of the proteolytic system of tetrahymena pyriformis W. II. Substrate specificity of constituent proteinases. Biochim Biophys Acta. 1962 Oct 8;64:52–59. doi: 10.1016/0006-3002(62)90759-x. [DOI] [PubMed] [Google Scholar]
  41. Davidson R., Gertler A., Hofmann T. Aspergillus oryzae acid proteinase. Purification and properties, and formation of pi-chymotrypsin. Biochem J. 1975 Apr;147(1):45–53. doi: 10.1042/bj1470045. [DOI] [PMC free article] [PubMed] [Google Scholar]
  42. De Toma F. J., Kindwall K. E., Reardon C. A. The effect of tosyl lysine chloromethyl ketone on the activity of uridine diphosphoglucose pyrophosphorylase of the cellular slime mold Dictyostelium discoideum. Biochem Biophys Res Commun. 1977 Jan 24;74(2):350–355. doi: 10.1016/0006-291x(77)90311-4. [DOI] [PubMed] [Google Scholar]
  43. Dobberstein B., Blobel G., Chua N. H. In vitro synthesis and processing of a putative precursor for the small subunit of ribulose-1,5-bisphosphate carboxylase of Chlamydomonas reinhardtii. Proc Natl Acad Sci U S A. 1977 Mar;74(3):1082–1085. doi: 10.1073/pnas.74.3.1082. [DOI] [PMC free article] [PubMed] [Google Scholar]
  44. Doonan S., Fahmy H. M. Specific enzymic cleavage of polypeptides at cysteine residues. Eur J Biochem. 1975 Aug 15;56(2):421–426. doi: 10.1111/j.1432-1033.1975.tb02248.x. [DOI] [PubMed] [Google Scholar]
  45. Drucker H. Regulation of exocellular proteases in Neurospora crassa: role of Neurospora proteases in induction. J Bacteriol. 1973 Nov;116(2):593–599. doi: 10.1128/jb.116.2.593-599.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  46. Ebeling W., Hennrich N., Klockow M., Metz H., Orth H. D., Lang H. Proteinase K from Tritirachium album Limber. Eur J Biochem. 1974 Aug 15;47(1):91–97. doi: 10.1111/j.1432-1033.1974.tb03671.x. [DOI] [PubMed] [Google Scholar]
  47. Firtel R. A., Brackenbruy R. W. Partial characterization of several protein and amino acid metabolizing enzymes in the cellular slime mold Dictyostelium discoideum. Dev Biol. 1972 Mar;27(3):307–321. doi: 10.1016/0012-1606(72)90170-4. [DOI] [PubMed] [Google Scholar]
  48. Fischer E. P., Thomson K. S. Serine proteinases and their inhibitors in Phycomyces blakesleeanus. J Biol Chem. 1979 Jan 10;254(1):50–56. [PubMed] [Google Scholar]
  49. Fong D., Bonner J. T. Proteases in cellular slime mold development: evidence for their involvement. Proc Natl Acad Sci U S A. 1979 Dec;76(12):6481–6485. doi: 10.1073/pnas.76.12.6481. [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Fong D., Rutherford C. L. Protease activity during cell differentiation of the cellular slime mold Dictyostelium discoideum. J Bacteriol. 1978 May;134(2):521–527. doi: 10.1128/jb.134.2.521-527.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  51. Franke J., Sussman M. Accumulation of uridine diphosphoglucose pyrophosphorylase in Dictyostelium discoideum via preferential synthesis. J Mol Biol. 1973 Dec 5;81(2):173–185. doi: 10.1016/0022-2836(73)90187-3. [DOI] [PubMed] [Google Scholar]
  52. Franke R. G., Berry J. A. Taxonomic application of isozyme patterns produced with disc electrophoresis of some myxomycetes, order Physarales. Mycologia. 1972 Jul-Aug;64(4):830–840. [PubMed] [Google Scholar]
  53. Galkin A. V., Tsoi T. V., Luzikov V. N. Abnormalities in mitochondrial respiratory chain assembly and their proteolytic elimination. FEBS Lett. 1979 Jul 1;103(1):111–113. doi: 10.1016/0014-5793(79)81261-2. [DOI] [PubMed] [Google Scholar]
  54. Germaine G. R., Tellefson L. M. Effect of pH and human saliva on protease production by Candida albicans. Infect Immun. 1981 Jan;31(1):323–326. doi: 10.1128/iai.31.1.323-326.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  55. Germaine G. R., Tellefson L. M., Johnson G. L. Proteolytic activity of Candida albicans: action on human salivary proteins. Infect Immun. 1978 Dec;22(3):861–866. doi: 10.1128/iai.22.3.861-866.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. Gibson W., Mehlitz D., Lanham S. M., Godfrey D. G. The identification of Trypanosoma brucei gambiense in Liberian pigs and dogs by isoenzymes and by resistance to human plasma. Tropenmed Parasitol. 1978 Sep;29(3):335–345. [PubMed] [Google Scholar]
  57. González-Garza M. T., Arellano-Blanco J., Gómez-Estrada H. Marcaje citoquímico de las enzimas proteolíticas de Entamoeba histolytica. Arch Invest Med (Mex) 1977;8(2):139–144. [PubMed] [Google Scholar]
  58. Grappel S. F. Role of keratinases in dermatophytosis. IV. Reactivities of sera from guinea pigs with heat-inactivated keratinase II. Dermatologica. 1976;153(3):157–162. [PubMed] [Google Scholar]
  59. Gripon J. C., Auberger B., Lenoir J. Metalloproteases from Penicillium caseicolum and P. roqueforti: comparison of specificity and chemical characterization. Int J Biochem. 1980;12(3):451–455. doi: 10.1016/0020-711x(80)90127-5. [DOI] [PubMed] [Google Scholar]
  60. Gripon J. C., Hofmann T. Inactivation of aspartyl proteinases by butane-2,3-dione. Modification of tryptophan and tyrosine residues and evidence against reaction of arginine residues. Biochem J. 1981 Jan 1;193(1):55–65. doi: 10.1042/bj1930055. [DOI] [PMC free article] [PubMed] [Google Scholar]
  61. Gripon J. C., Rhee S. H., Hofmann T. N-terminal amino acid sequences of acid proteases: acid proteases from Penicillium roqueforti and Rhizopus chinensis and alignment with penicillopepsin and mammalian proteases. Can J Biochem. 1977 May;55(5):504–506. doi: 10.1139/o77-071. [DOI] [PubMed] [Google Scholar]
  62. Groninger H. S., Jr, Eklund M. W. Characteristics of a proteinase of a trichosporon species isolated from Dungeness crab meat. Appl Microbiol. 1966 Jan;14(1):110–114. doi: 10.1128/am.14.1.110-114.1966. [DOI] [PMC free article] [PubMed] [Google Scholar]
  63. Gustafson G. L., Milner L. A. Immunological relationship between beta-N-acetyglucosaminidase and proteinase I from Dictyostelium discoideum. Biochem Biophys Res Commun. 1980 Jun 30;94(4):1439–1444. doi: 10.1016/0006-291x(80)90580-x. [DOI] [PubMed] [Google Scholar]
  64. Gustafson G. L., Milner L. A. Occurrence of N-acetylglucosamine-1-phosphate in proteinase I from Dictyostelium discoideum. J Biol Chem. 1980 Aug 10;255(15):7208–7210. [PubMed] [Google Scholar]
  65. Gustafson G. L., Thon L. A. Purification and characterization of a proteinase from Dictyostelium discoideum. J Biol Chem. 1979 Dec 25;254(24):12471–12478. [PubMed] [Google Scholar]
  66. HARINASUTA C., MAEGRAITH B. G. The demonstration of proteolytic enzyme activity of Entamoeba histolytica by the use of photographic gelatin film. Ann Trop Med Parasitol. 1958 Dec;52(4):508–515. doi: 10.1080/00034983.1958.11685888. [DOI] [PubMed] [Google Scholar]
  67. HARTLEY B. S. Proteolytic enzymes. Annu Rev Biochem. 1960;29:45–72. doi: 10.1146/annurev.bi.29.070160.000401. [DOI] [PubMed] [Google Scholar]
  68. Hanson M. A., Marzluf G. A. Control of the synthesis of a single enzyme by multiple regulatory circuits in Neurospora crassa. Proc Natl Acad Sci U S A. 1975 Apr;72(4):1240–1244. doi: 10.1073/pnas.72.4.1240. [DOI] [PMC free article] [PubMed] [Google Scholar]
  69. Hasilik A., Tanner W. Biosynthesis of the vacuolar yeast glycoprotein carboxypeptidase Y. Conversion of precursor into the enzyme. Eur J Biochem. 1978 Apr 17;85(2):599–608. doi: 10.1111/j.1432-1033.1978.tb12275.x. [DOI] [PubMed] [Google Scholar]
  70. Hayashi R., Moore S., Stein W. H. Carboxypeptidase from yeast. Large scale preparation and the application to COOH-terminal analysis of peptides and proteins. J Biol Chem. 1973 Apr 10;248(7):2296–2302. [PubMed] [Google Scholar]
  71. Hemmings B. A., Zubenko G. S., Hasilik A., Jones E. W. Mutant defective in processing of an enzyme located in the lysosome-like vacuole of Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 1981 Jan;78(1):435–439. doi: 10.1073/pnas.78.1.435. [DOI] [PMC free article] [PubMed] [Google Scholar]
  72. Hemmings B. A., Zubenko G. S., Jones E. W. Proteolytic inactivation of the NADP-dependent glutamate dehydrogenase in proteinase-deficient mutants of Saccharomyces cerevisiae. Arch Biochem Biophys. 1980 Jul;202(2):657–660. doi: 10.1016/0003-9861(80)90475-0. [DOI] [PubMed] [Google Scholar]
  73. Hempelmann E., Wilson R. J. Endopeptidases from Plasmodium knowlesi. Parasitology. 1980 Apr;80(2):323–330. doi: 10.1017/s0031182000000780. [DOI] [PubMed] [Google Scholar]
  74. Henney H. R., Jr, Maxey G. Nutritional control of differentiation (sclerotization) of the myxomycete Physarum flavicomum. Can J Biochem. 1975 Jul;53(7):810–818. doi: 10.1139/o75-109. [DOI] [PubMed] [Google Scholar]
  75. Hernández-Jodra M., Gancedo C. Characterization of an intracellular inhibitor of the carboxypeptidase R from Rhodotorula glutinis. Hoppe Seylers Z Physiol Chem. 1979 Jul;360(7):913–917. doi: 10.1515/bchm2.1979.360.2.913. [DOI] [PubMed] [Google Scholar]
  76. Hoffmann W., Hüttermann A. Aminopeptidases of Physarum polycephalum. Activity, isoenzyme pattern, and synthesis during differentiation. J Biol Chem. 1975 Sep 25;250(18):7420–7427. [PubMed] [Google Scholar]
  77. Holzer H., Betz H., Ebner E. Intracellular proteinases in microorganisms. Curr Top Cell Regul. 1975;9:103–156. doi: 10.1016/b978-0-12-152809-6.50011-1. [DOI] [PubMed] [Google Scholar]
  78. Holzer H., Heinrich P. C. Control of proteolysis. Annu Rev Biochem. 1980;49:63–91. doi: 10.1146/annurev.bi.49.070180.000431. [DOI] [PubMed] [Google Scholar]
  79. Holzer H. Initiation of selective proteolysis by metabolic interconversion. Acta Biol Med Ger. 1981;40(10-11):1393–1396. [PubMed] [Google Scholar]
  80. Houmard J., Raymond M. N. Further characterization of the Penicillium roqueforti acid protease. Biochimie. 1979;61(8):979–982. doi: 10.1016/s0300-9084(79)80250-3. [DOI] [PubMed] [Google Scholar]
  81. Hsu I. N., Delbaere L. T., James M. N., Hofmann T. Penicillopepsin from Penicillium janthinellum crystal structure at 2.8 A and sequence homology with porcine pepsin. Nature. 1977 Mar 10;266(5598):140–145. doi: 10.1038/266140a0. [DOI] [PubMed] [Google Scholar]
  82. Hwang J., Hseu T. H. Specificity of the acid protease from Monascus kaoliang towards the B-chain of oxidized insulin. Biochim Biophys Acta. 1980 Aug 7;614(2):607–612. doi: 10.1016/0005-2744(80)90250-8. [DOI] [PubMed] [Google Scholar]
  83. Iio K., Yamasaki M. Specificity of acid proteinase A from Aspergillus niger var. macrosporus towards B-chain of performic acid oxidized bovine insulin. Biochim Biophys Acta. 1976 May 13;429(3):912–924. doi: 10.1016/0005-2744(76)90336-3. [DOI] [PubMed] [Google Scholar]
  84. Impoolsup A., Bhumiratana A., Flegel T. W. Isolation of Alkaline and Neutral Proteases from Aspergillus flavus var. columnaris, a Soy Sauce Koji Mold. Appl Environ Microbiol. 1981 Oct;42(4):619–628. doi: 10.1128/aem.42.4.619-628.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Itow S., Camargo E. P. Proteolytic activites in cell extracts of Trypanosoma cruzi. J Protozool. 1977 Nov;24(4):591–595. doi: 10.1111/j.1550-7408.1977.tb01021.x. [DOI] [PubMed] [Google Scholar]
  86. JARUMILINTA R., MAEGRAITH B. G. The patterns of some proteolytic enzymes of Entamoeba histolytica and Acanthamoeba sp. I. The action of E. histolytica and Acanthamoeba sp. on protein substrates. Ann Trop Med Parasitol. 1961 Dec;55:505–517. doi: 10.1080/00034983.1961.11686080. [DOI] [PubMed] [Google Scholar]
  87. JARUMILINTA R., MAEGRAITH B. G. The patterns of some proteolytic enzymes of Entamoeba histolytica and Acanthamoeba sp. II. The action E. histolytica and acanthamoeba sp. on various synthetic substrates. Ann Trop Med Parasitol. 1961 Dec;55:518–528. [PubMed] [Google Scholar]
  88. Johnson G. L., Brown J. L. Partial purification and characterization of two peptidases from Neurospora crassa. Biochim Biophys Acta. 1974 Dec 29;370(2):530–540. doi: 10.1016/0005-2744(74)90114-4. [DOI] [PubMed] [Google Scholar]
  89. Jones E. W. Proteinase mutants of Saccharomyces cerevisiae. Genetics. 1977 Jan;85(1):23–33. doi: 10.1093/genetics/85.1.23. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Jönsson A. G. Purification and some properties of a protease from Alternaria tenuissima. Arch Biochem Biophys. 1969 Jan;129(1):62–67. doi: 10.1016/0003-9861(69)90150-7. [DOI] [PubMed] [Google Scholar]
  91. Kaushal D. C., Shukla O. P. Elaboration of proteases, cellulase & chitinase during excystment of Hartmannella culbertsoni. Indian J Exp Biol. 1978 Oct;16(10):1104–1106. [PubMed] [Google Scholar]
  92. Kaushal D. C., Shukla O. P. Excystment of axenically prepared cysts of Hartmanella culbertsoni. J Gen Microbiol. 1977 Jan;98(1):117–123. doi: 10.1099/00221287-98-1-117. [DOI] [PubMed] [Google Scholar]
  93. Kaushal D. C., Shukla O. P. Properties of an extracellular protease elaborated during excystment of Hartmannella culbertsoni. Indian J Exp Biol. 1978 Oct;16(10):1102–1104. [PubMed] [Google Scholar]
  94. Kaushal D. C., Shukla O. P. Release of certain extracellular enzymes during excystment of axenically produced cysts of hartmannella culbertsoni. Indian J Exp Biol. 1976 Jul;14(4):498–499. [PubMed] [Google Scholar]
  95. Kauss H., Thomson K. S., Tetour M., Jeblick W. Proteolytic activation of a galactosyl transferase involved in osmotic regulation. Plant Physiol. 1978 Jan;61(1):35–37. doi: 10.1104/pp.61.1.35. [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Kinsella J. E., Hwang D. H. Enzymes of Penicillium roqueforti involved in the biosynthesis of cheese flavor. CRC Crit Rev Food Sci Nutr. 1976 Nov;8(2):191–228. doi: 10.1080/10408397609527222. [DOI] [PubMed] [Google Scholar]
  97. Klapper B. F., Jameson D. M., Mayer R. M. Factors affecting the synthesis and release of the extracellular protease of Aspergillus oryzae NRRL 2160. Biochim Biophys Acta. 1973 Apr 28;304(2):513–519. doi: 10.1016/0304-4165(73)90271-7. [DOI] [PubMed] [Google Scholar]
  98. Klar A. J., Halvorson H. O. Proteinase activities of Saccharomyces cerevisiae during sporulation. J Bacteriol. 1975 Nov;124(2):863–869. doi: 10.1128/jb.124.2.863-869.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  99. Knecht D. A., Dimond R. L. Lysosomal enzymes possess a common antigenic determinant in the cellular slime mold, Dictyostelium discoideum. J Biol Chem. 1981 Apr 10;256(7):3564–3575. [PubMed] [Google Scholar]
  100. Kominami E., Hoffschulte H., Leuschel L., Maier K., Holzer H. The substrate specificity of proteinase B from baker's yeast. Biochim Biophys Acta. 1981 Sep 15;661(1):136–141. doi: 10.1016/0005-2744(81)90092-9. [DOI] [PubMed] [Google Scholar]
  101. Kovaleva G. G., Shimanskaya M. P., Stepanov V. M. The site of diazoacetyl inhibitor attachment to acid proteinase of Aspergillus awamori--an analog of penicillopepsin and pepsin. Biochem Biophys Res Commun. 1972 Nov 15;49(4):1075–1081. doi: 10.1016/0006-291x(72)90322-1. [DOI] [PubMed] [Google Scholar]
  102. Kreil G. Transfer of proteins across membranes. Annu Rev Biochem. 1981;50:317–348. doi: 10.1146/annurev.bi.50.070181.001533. [DOI] [PubMed] [Google Scholar]
  103. Kucera M. [Toxins of the entomophagous fungus Beauveria bassiana. II. Effect of nitrogen sources on formation of the toxic protease in submerged culture]. J Invertebr Pathol. 1971 Mar;17(2):211–215. doi: 10.1016/0022-2011(71)90093-0. [DOI] [PubMed] [Google Scholar]
  104. Kumar C. C., Padmanaban G. Evidence for the involvement of a rapidly turning over protease in the degradation of cytochrome oxidase in Neurospora crassa. Biochem Biophys Res Commun. 1981 May 29;100(2):576–583. doi: 10.1016/s0006-291x(81)80215-x. [DOI] [PubMed] [Google Scholar]
  105. Kundu A. K., Manna S., Pal N. Purification and properties of a new extracellular collagenase from Aspergillus sclerotiorum. Indian J Exp Biol. 1974 Sep;12(5):441–443. [PubMed] [Google Scholar]
  106. Kundu A. K., Manna S. Purification and characterization of extracellular proteinases of Aspergillus oryzae. Appl Microbiol. 1975 Oct;30(4):507–513. doi: 10.1128/am.30.4.507-513.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  107. Labarere J., Bernet J. Protoplasmic Incompatibility in PODOSPORA ANSERINA: A Possible Role for Its Associated Proteolytic Activity. Genetics. 1979 Nov;93(3):525–537. doi: 10.1093/genetics/93.3.525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Langner J., Wiederanders B., Ansorge S., Bohley P., Kirschke The ribosomal serine proteinase: cathepsin R. Acta Biol Med Ger. 1979;38(11-12):1527–1538. [PubMed] [Google Scholar]
  109. Lawrie N. R. Studies in the metabolism of protozoa: Some biochemical reactions occurring in the presence of the washed cells of Glaucoma pyriformis. Biochem J. 1935 Oct;29(10):2297–2302. doi: 10.1042/bj0292297. [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Lawrie N. R. Studies in the metabolism of protozoa: Some properties of a proteolytic extract obtained from Glaucoma piriformis. Biochem J. 1937 May;31(5):789–798. doi: 10.1042/bj0310789. [DOI] [PMC free article] [PubMed] [Google Scholar]
  111. Lenney J. F. Three yeast proteins that specifically inhibit yeast proteases A, B, and C. J Bacteriol. 1975 Jun;122(3):1265–1273. doi: 10.1128/jb.122.3.1265-1273.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. Lenz A. G., Holzer H. Rapid reversible inactivation of fructose-1,6-bisphosphatase in Saccharomyces cerivisiae by glucose. FEBS Lett. 1980 Jan 14;109(2):271–274. doi: 10.1016/0014-5793(80)81103-3. [DOI] [PubMed] [Google Scholar]
  113. Letch C. A., Gibson W. Trypanosoma brucei: the peptidases of bloodstream trypanosomes. Exp Parasitol. 1981 Aug;52(1):86–90. doi: 10.1016/0014-4894(81)90064-3. [DOI] [PubMed] [Google Scholar]
  114. Levy M. R., Chou S. C. Activity and some properties of an acid proteinase from normal and Plasmodium berghei-infected red cells. J Parasitol. 1973 Dec;59(6):1064–1070. [PubMed] [Google Scholar]
  115. Levy M. R., McConkey C. L. Enzyme inactivation by a cellular neutral protease: enzyme specificity, effects of ligands on inactivation, and implications for the regulation of enzyme degradation. J Cell Physiol. 1977 Feb;90(2):253–263. doi: 10.1002/jcp.1040900211. [DOI] [PubMed] [Google Scholar]
  116. Levy M. R., Siddiqui W. A., Chou S. C. Acid protease activity in Plasmodium falciparum and P. knowlesi and ghosts of their respective host red cells. Nature. 1974 Feb 22;247(5442):546–549. doi: 10.1038/247546a0. [DOI] [PubMed] [Google Scholar]
  117. Levy M. R., Sisskin E. E., McConkey C. L. A protease that increases during a period of enzymic and metabolic adjustment in Tetrahymena. Arch Biochem Biophys. 1976 Feb;172(2):634–647. doi: 10.1016/0003-9861(76)90118-1. [DOI] [PubMed] [Google Scholar]
  118. Lewis W. G., Basford J. M., Walton P. L. Specificity and inhibition studies of Armillaria mellea protease. Biochim Biophys Acta. 1978 Feb 10;522(2):551–560. doi: 10.1016/0005-2744(78)90087-6. [DOI] [PubMed] [Google Scholar]
  119. Lindberg R. A., Eirich L. D., Price J. S., Wolfinbarger L., Jr, Drucker H. Alkaline protease from Neurospora crassa. Purification and partial characterization. J Biol Chem. 1981 Jan 25;256(2):811–814. [PubMed] [Google Scholar]
  120. Lindmark D. G., Müller M. Biochemical cytology of trichomonad flagellates. II. Subcellular distribution of oxidoreductases and hydrolases in Monocercomonas sp. J Protozool. 1974 May;21(2):374–378. doi: 10.1111/j.1550-7408.1974.tb03673.x. [DOI] [PubMed] [Google Scholar]
  121. Liu C. L., Hatano H. An aspartic acid residue at the active site of Rhodotorula glutinis acid protease. FEBS Lett. 1974 Jun 15;42(3):352–354. doi: 10.1016/0014-5793(74)80763-5. [DOI] [PubMed] [Google Scholar]
  122. Lodi W. R., Sonneborn D. R. Protein degradation and protease activity during the late cycle of Blastocladiella emersonii. J Bacteriol. 1974 Mar;117(3):1035–1042. doi: 10.1128/jb.117.3.1035-1042.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  123. Macdonald F., Odds F. C. Inducible proteinase of Candida albicans in diagnostic serology and in the pathogenesis of systemic candidosis. J Med Microbiol. 1980 Aug;13(3):423–435. doi: 10.1099/00222615-13-3-423. [DOI] [PubMed] [Google Scholar]
  124. Macdonald F., Odds F. C. Purified Candida albicans proteinase in the serological diagnosis of systemic candidosis. JAMA. 1980 Jun 20;243(23):2409–2411. [PubMed] [Google Scholar]
  125. Mahoney J. R., Eaton J. W. Chloroquine resistant malaria: association with enhanced plasmodial protease activity. Biochem Biophys Res Commun. 1981 Jun 16;100(3):1266–1271. doi: 10.1016/0006-291x(81)91960-4. [DOI] [PubMed] [Google Scholar]
  126. Maier K., Müller H., Tesch R., Trolp R., Witt I., Holzer H. Primary structure of yeast proteinase B inhibitor 2. J Biol Chem. 1979 Dec 25;254(24):12555–12561. [PubMed] [Google Scholar]
  127. Martin P., Raymond M. N., Bricas E., Dumas B. R. Kinetic studies on the action of Mucor pusillus, Mucor miehei acid proteases and chymosins A and B on a synthetic chromophoric hexapeptide. Biochim Biophys Acta. 1980 Apr 11;612(2):410–420. doi: 10.1016/0005-2744(80)90124-2. [DOI] [PubMed] [Google Scholar]
  128. Matsushima K. I. A note on a novel fungal alkaline proteinase inhibitor from Aspergillus oryzae. Biochem Biophys Res Commun. 1979 Oct 29;90(4):1142–1146. doi: 10.1016/0006-291x(79)91155-0. [DOI] [PubMed] [Google Scholar]
  129. McLaughlin J., Faubert G. Partial purification and some properties of a neutral sulfhydryl and an acid proteinase from Entamoeba histolytica. Can J Microbiol. 1977 Apr;23(4):420–425. doi: 10.1139/m77-062. [DOI] [PubMed] [Google Scholar]
  130. McLaughlin J., Müller M. Purification and characterization of a low molecular weight thiol proteinase from the flagellate protozoon Tritrichomonas foetus. J Biol Chem. 1979 Mar 10;254(5):1526–1533. [PubMed] [Google Scholar]
  131. McMurrough I., Bartnicki-Garcia S. Inhibition and activation of chitin synthesis by Mucor rouxii cell extracts. Arch Biochem Biophys. 1973 Oct;158(2):812–816. doi: 10.1016/0003-9861(73)90576-6. [DOI] [PubMed] [Google Scholar]
  132. Mechler B., Wolf D. H. Analysis of proteinase A function in yeast. Eur J Biochem. 1981 Dec;121(1):47–52. doi: 10.1111/j.1432-1033.1981.tb06427.x. [DOI] [PubMed] [Google Scholar]
  133. Meevootisom V., Niederpruem D. J. Control of exocellular proteases in dermatophytes and especially Trichophyton rubrum. Sabouraudia. 1979 Jun;17(2):91–106. doi: 10.1080/00362177985380141. [DOI] [PubMed] [Google Scholar]
  134. Michel R., Liebl A., Hartmann A., Neupert W. Action of intracellular proteinases on mitochondrial translation products of Neurospora crassa Schizosaccharomyces pombe. Hoppe Seylers Z Physiol Chem. 1976 Mar;357(3):415–426. doi: 10.1515/bchm2.1976.357.1.415. [DOI] [PubMed] [Google Scholar]
  135. Mikes O., Turková J., Toan N. B., Sorm F. Serine-containing active center of alkaline proteinase of Aspergillus flavus. Biochim Biophys Acta. 1969 Mar 18;178(1):112–117. doi: 10.1016/0005-2744(69)90137-5. [DOI] [PubMed] [Google Scholar]
  136. Minocha Y., Pasricha J. S., Mohapatra L. N., Kandhari K. C. Proteolytic activity of dermatophytes and its role in the pathogenesis of skin lesions. Sabouraudia. 1972 Mar;10(1):79–85. doi: 10.1080/00362177285190161. [DOI] [PubMed] [Google Scholar]
  137. Morihara K. Comparative specificity of microbial proteinases. Adv Enzymol Relat Areas Mol Biol. 1974;41(0):179–243. doi: 10.1002/9780470122860.ch5. [DOI] [PubMed] [Google Scholar]
  138. Morihara K., Oka T. Comparative specificity of microbial acid proteinases for synthetic peptides. 3. Relationship with their trypsinogen activating ability. Arch Biochem Biophys. 1973 Aug;157(2):561–572. doi: 10.1016/0003-9861(73)90675-9. [DOI] [PubMed] [Google Scholar]
  139. Morihara K., Tsuzuki H., Murao S., Oda K. Pepstatin-insenstive acid proteases from Scytalidium lignicolum. Kinetic study with synthetic peptides. J Biochem. 1979 Mar;85(3):661–668. [PubMed] [Google Scholar]
  140. Murakami T., Suzuki Y., Murachi T. An acid protease in human erythrocytes and its localization in the inner membrane. Eur J Biochem. 1979 May 15;96(2):221–227. doi: 10.1111/j.1432-1033.1979.tb13032.x. [DOI] [PubMed] [Google Scholar]
  141. Müller M., Müller H., Holzer H. Immunochemical studies on catabolite inactivation of phosphoenolpyruvate carboxykinase in Saccharomyces cerevisiae. J Biol Chem. 1981 Jan 25;256(2):723–727. [PubMed] [Google Scholar]
  142. Müller M., Müller H. Synthesis and processing of in vitro and in vivo precursors of the vacuolar yeast enzyme carboxypeptidase Y. J Biol Chem. 1981 Dec 10;256(23):11962–11965. [PubMed] [Google Scholar]
  143. NAKAMURA M., EDWARDS P. R., Jr Casease in Entamoeba histolytica. Nature. 1959 Feb 7;183(4658):397–397. doi: 10.1038/183397b0. [DOI] [PubMed] [Google Scholar]
  144. NEAL R. A. Enzymic proteolysis by Entamoeba histolytica; biochemical characteristics and relationship with invasiveness. Parasitology. 1960 Nov;50:531–550. doi: 10.1017/s0031182000025610. [DOI] [PubMed] [Google Scholar]
  145. Nakamura S., Takahashi K. The structure and function of acid proteases. IX. Isolation and amino acid sequences of the peptides containing the active site aspartyl residues reactive with diazoacetyl-DL-norleucine methyl ester and 1,2-epoxy-3-(p-nitrophenoxy)propane in Rhizopus chinensis acid protease. J Biochem. 1978 Dec;84(6):1593–1600. doi: 10.1093/oxfordjournals.jbchem.a132285. [DOI] [PubMed] [Google Scholar]
  146. Nakayama S., Nagashima Y., Hoshino M., Moriyama A., Takahashi K., Uematsu Y., Watanabe T., Yoshida M. Spin-labeling of porcine pepsin and Rhizopus chinensis acid protease by diazoketone reagents. Biochem Biophys Res Commun. 1981 Jul 30;101(2):658–662. doi: 10.1016/0006-291x(81)91309-7. [DOI] [PubMed] [Google Scholar]
  147. North M. J., Coombs G. H. Proteinases of Leishmania mexicana amastigotes and promastigotes: analysis by gel electrophoresis. Mol Biochem Parasitol. 1981 Sep;3(5):293–300. doi: 10.1016/0166-6851(81)90003-7. [DOI] [PubMed] [Google Scholar]
  148. North M. J., Harwood J. M. Multiple acid proteinases in the cellular slime mould Dictyostelium discoideum. Biochim Biophys Acta. 1979 Jan 12;566(1):222–233. doi: 10.1016/0005-2744(79)90264-x. [DOI] [PubMed] [Google Scholar]
  149. North M. J. Inhibition of acid proteinase from Dictyostelium discoideum [proceedings]. Biochem Soc Trans. 1978;6(2):400–403. doi: 10.1042/bst0060400. [DOI] [PubMed] [Google Scholar]
  150. Novikova L. A., Zubatov A. S., Luzikov V. N. Multiplicity of mitochondrial proteinases in yeast. FEBS Lett. 1981 Dec 7;135(2):245–248. doi: 10.1016/0014-5793(81)80792-2. [DOI] [PubMed] [Google Scholar]
  151. O'Day D. H. Acid protease activity during germination of microcysts of the cellular slime mold Polysphondylium pallidum. J Bacteriol. 1976 Jan;125(1):8–13. doi: 10.1128/jb.125.1.8-13.1976. [DOI] [PMC free article] [PubMed] [Google Scholar]
  152. O'Day D. H. Intracellular and extracellular enzyme patterns during microcyst germination in the cellular slime mold Polysphondylium pallidum. Dev Biol. 1974 Feb;36(2):400–410. doi: 10.1016/0012-1606(74)90061-x. [DOI] [PubMed] [Google Scholar]
  153. O'Sullivan J., Mathison G. E. The localization and secretion of a propteolytic enzyme complex by the dermatophytic fungus Microsporum canis. J Gen Microbiol. 1971 Nov;68(3):319–326. doi: 10.1099/00221287-68-3-319. [DOI] [PubMed] [Google Scholar]
  154. Ogrydziak D. M., Demain A. L., Tannenbaum S. R. Regulation of extracellular protease production in Candida lipolytica. Biochim Biophys Acta. 1977 Apr 27;497(2):525–538. doi: 10.1016/0304-4165(77)90209-4. [DOI] [PubMed] [Google Scholar]
  155. Opheim D. J. Effect of ammonium ions on activity of hydrolytic enzymes during sporulation of yeast. J Bacteriol. 1979 Jun;138(3):1022–1025. doi: 10.1128/jb.138.3.1022-1025.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  156. Page W. J., Stock J. J. Isolation and characterization of Microsporum gypseum lysosomes: role of lysosomes in macroconidia germination. J Bacteriol. 1972 Apr;110(1):354–362. doi: 10.1128/jb.110.1.354-362.1972. [DOI] [PMC free article] [PubMed] [Google Scholar]
  157. Page W. J., Stock J. J. Phosphate-mediated alteration of the Microsporum gypseum germination protease specificity for substrate: enhanced keratinase activity. J Bacteriol. 1974 Feb;117(2):422–431. doi: 10.1128/jb.117.2.422-431.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  158. Panneerselvam M., Dhar S. C. Studies on the peptide bond specificity and the essential groups of an acid proteinase from Aspergillus fumigatus. Ital J Biochem. 1981 May-Jun;30(3):207–216. [PubMed] [Google Scholar]
  159. Panneerselvan M., Dhar S. C. Trypsinogen-kinase from Aspergillus fumigatus. Experientia. 1980 Apr 15;36(4):387–388. doi: 10.1007/BF01975102. [DOI] [PubMed] [Google Scholar]
  160. Pauling K. D., Jones G. E. Asparaginase II of Saccharomyces cerevisiae: inactivation during the transition to stationary phase. Biochim Biophys Acta. 1980 Dec 4;616(2):271–282. doi: 10.1016/0005-2744(80)90144-8. [DOI] [PubMed] [Google Scholar]
  161. Polanshek M. M., Blomquist J. C., Evans T. E., Rusch H. P. Aminopeptidases of Physarum polycephalum during growth and differentiation. Arch Biochem Biophys. 1978 Sep;190(1):261–269. doi: 10.1016/0003-9861(78)90275-8. [DOI] [PubMed] [Google Scholar]
  162. Pong S. S., Nuss D. L., Koch G. Inhibition of initiation of protein synthesis in mammalian tissue culture cells by L-1-tosylamido-2-phenylethyl chloromethyl ketone. J Biol Chem. 1975 Jan 10;250(1):240–245. [PubMed] [Google Scholar]
  163. Pontremoli S., Salamino F., Sparatore B., Melloni E., Morelli A., Benatti U., De Flora A. Isolation and partial characterization of three acidic proteinases in erythrocyte membranes. Biochem J. 1979 Sep 1;181(3):559–568. doi: 10.1042/bj1810559. [DOI] [PMC free article] [PubMed] [Google Scholar]
  164. Pontremoli S., Sparatore B., Melloni E., Salamino F., Michetti M., Morelli A., Benatti U., de Flora A. Differences and similarities among three acidic endopeptidases associated with human erythrocyte membranes. Molecular and functional studies. Biochim Biophys Acta. 1980 Jul 3;630(3):313–322. doi: 10.1016/0304-4165(80)90279-2. [DOI] [PubMed] [Google Scholar]
  165. Rangel H. A., Araújo P. M., Camargo I. J., Bonfitto M., Repka D., Sakurada J. K., Atta A. M. Detection of a proteinase common to epimastigote, trypomastigote and amastigote of different strains of Trypanosoma cruzi. Tropenmed Parasitol. 1981 Jun;32(2):87–92. [PubMed] [Google Scholar]
  166. Rangel H. A., Araújo P. M., Repka D., Costa M. G. Trypanosoma cruzi: isolation and characterization of a proteinase. Exp Parasitol. 1981 Oct;52(2):199–209. doi: 10.1016/0014-4894(81)90075-8. [DOI] [PubMed] [Google Scholar]
  167. Reichelt D., Jacobsohn E., Haschen R. J. Purification and properties of cathepsin D from human erythrocytes. Biochim Biophys Acta. 1974 Mar 21;341(1):15–26. doi: 10.1016/0005-2744(74)90061-8. [DOI] [PubMed] [Google Scholar]
  168. Remold H., Fasold H., Staib F. Purification and characterization of a proteolytic enzyme from Candida albicans. Biochim Biophys Acta. 1968 Oct 8;167(2):399–406. doi: 10.1016/0005-2744(68)90219-2. [DOI] [PubMed] [Google Scholar]
  169. Ricketts T. R., Rappitt A. F. Endocytosis and the adaptive acid hydrolases in Tetrahymena pyriformis GL. Arch Microbiol. 1974 Jul 4;98(2):115–126. doi: 10.1007/BF00425274. [DOI] [PubMed] [Google Scholar]
  170. Rigby D. J., Radford A. The involvement of proteolysis in conformational stability of the carbamoyl-phosphate synthetase/aspartate carbamoyltransferase enzyme of Neurospora crassa. Biochim Biophys Acta. 1981 Oct 13;661(2):315–322. doi: 10.1016/0005-2744(81)90020-6. [DOI] [PubMed] [Google Scholar]
  171. Rippon J. W., Varadi D. P. The elastases of pathogenic fungi and actinomycetes. J Invest Dermatol. 1968 Jan;50(1):54–58. doi: 10.1038/jid.1968.8. [DOI] [PubMed] [Google Scholar]
  172. Roberts F. F., Doetsch R. N. Purification of a highly active protease from a Microsporum species. Antonie Van Leeuwenhoek. 1967;33(2):145–152. doi: 10.1007/BF02045544. [DOI] [PubMed] [Google Scholar]
  173. Robinson N. C., Neurath H., Walsh K. A. Preparation and characterization of guanidinated trypsinogen and -guanidinated trypsin. Biochemistry. 1973 Jan 30;12(3):414–420. doi: 10.1021/bi00727a009. [DOI] [PubMed] [Google Scholar]
  174. Rossman T., Norris C., Troll W. Inhibition of macromolecular synthesis in Escherichia coli by protease inhibitors. Specific reversal by glutathione of the effects of chloromethyl ketones. J Biol Chem. 1974 Jun 10;249(11):3412–3417. [PubMed] [Google Scholar]
  175. Rossomando E. F., Maldonado B., Crean E. V., Kollar E. J. Protease secretion during onset of development in Dictyostelium discoideum. J Cell Sci. 1978 Apr;30:305–318. doi: 10.1242/jcs.30.1.305. [DOI] [PubMed] [Google Scholar]
  176. Royer G. P., Hsiao H. Y., Anantharamaiah G. M. Use of immobilized carboxypeptidase Y (I-CPY) as a catalyst for deblocking in peptide synthesis. Biochimie. 1980;62(8-9):537–541. doi: 10.1016/s0300-9084(80)80098-8. [DOI] [PubMed] [Google Scholar]
  177. Rüchel R. Properties of a purified proteinase from the yeast Candida albicans. Biochim Biophys Acta. 1981 May 14;659(1):99–113. doi: 10.1016/0005-2744(81)90274-6. [DOI] [PubMed] [Google Scholar]
  178. STEFANINI M., MARIN H. Fibrinolysis. I. Fibrinolytic activity of extracts from non-pathogenic fungi. Proc Soc Exp Biol Med. 1958 Nov;99(2):504–507. doi: 10.3181/00379727-99-24398. [DOI] [PubMed] [Google Scholar]
  179. Saheki T., Holzer H. Proteolytic activities in yeast. Biochim Biophys Acta. 1975 Mar 28;384(1):203–214. doi: 10.1016/0005-2744(75)90109-6. [DOI] [PubMed] [Google Scholar]
  180. Saltarelli C. G., Gentile K. A., Mancuso S. C. Lethality of Candida strains as influenced by the host. Can J Microbiol. 1975 May;21(5):648–654. doi: 10.1139/m75-093. [DOI] [PubMed] [Google Scholar]
  181. Samsináková A., Leopold H., Kálalová S. Der Abbau der Epidermis-Proteine der Raupe Galleria mellonella mittels der durch den entomophagen Pilz Beauveria bassiana sezernierten toxischen proteolytischen Enzyme. Zentralbl Bakteriol Parasitenkd Infektionskr Hyg. 1976;131(1):60–65. [PubMed] [Google Scholar]
  182. Schechter I., Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun. 1967 Apr 20;27(2):157–162. doi: 10.1016/s0006-291x(67)80055-x. [DOI] [PubMed] [Google Scholar]
  183. Schwalb M. N. Changes in activity of enzymes metabolizing glucose 6-phosphate during development of the basidiomycete Schizophyllum. Dev Biol. 1974 Sep;40(1):84–89. doi: 10.1016/0012-1606(74)90110-9. [DOI] [PubMed] [Google Scholar]
  184. Schwalb M. N. Developmentally regulated proteases from the basidiomycete Schizophyllum commune. J Biol Chem. 1977 Dec 10;252(23):8435–8439. [PubMed] [Google Scholar]
  185. Scott G. K., Kee T. B. Neutral proteases from human and ovine erythrocyte membranes. Int J Biochem. 1979;10(12):1039–1043. doi: 10.1016/0020-711x(79)90086-7. [DOI] [PubMed] [Google Scholar]
  186. Sharma S. K., Hopkins T. R. Activation of bovine chymotrypsinogen A. Isolation and characterization of mu- and omega-chymotrypsin. Biochemistry. 1979 Mar 20;18(6):1008–1013. doi: 10.1021/bi00573a012. [DOI] [PubMed] [Google Scholar]
  187. Shechter Y., Rafaeli-Eshkol D., Hershko A. Influence of protease inhibitors and energy metabolism on intracellular protein breakdown in starving Escherichia coli. Biochem Biophys Res Commun. 1973 Oct 15;54(4):1518–1524. doi: 10.1016/0006-291x(73)91158-3. [DOI] [PubMed] [Google Scholar]
  188. Sherman I. W. Amino acid metabolism and protein synthesis in malarial parasites. Bull World Health Organ. 1977;55(2-3):265–276. [PMC free article] [PubMed] [Google Scholar]
  189. Shimada K., Matsushima K., Fukumoto J., Yamamoto T. Poly-(L)-malic acid; a new protease inhibitor from Penicillium cyclopium. Biochem Biophys Res Commun. 1969 Jun 6;35(5):619–624. doi: 10.1016/0006-291x(69)90449-5. [DOI] [PubMed] [Google Scholar]
  190. Shipolini R. A., Callewaert G. L., Cottrell R. C., Vernon C. A. The amino-acid sequence and carbohydrate content of phospholipase A2 from bee venom. Eur J Biochem. 1974 Oct 2;48(2):465–476. doi: 10.1111/j.1432-1033.1974.tb03787.x. [DOI] [PubMed] [Google Scholar]
  191. Simms P. C., Ogrydziak D. M. Structural gene for the alkaline extracellular protease of Saccharomycopsis lipolytica. J Bacteriol. 1981 Jan;145(1):404–409. doi: 10.1128/jb.145.1.404-409.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  192. Steers E., Jr, Davis R. H., Jr A reexamination of the structure of the immobilization antigen from Paramecium aurelia. Comp Biochem Physiol B. 1977;56(2):195–199. doi: 10.1016/0305-0491(77)90048-7. [DOI] [PubMed] [Google Scholar]
  193. Steiger R. F., Opperdoes F. R., Bontemps J. Subcellular fractionation of Trypanosoma brucei bloodstream forms with special reference to hydrolases. Eur J Biochem. 1980 Mar;105(1):163–175. doi: 10.1111/j.1432-1033.1980.tb04486.x. [DOI] [PubMed] [Google Scholar]
  194. Stepanov V. M., Timokhina E. A., Zyakun A. M. Leucyl-pepsin a product of hog pepsinogen activation by proteinases of aspergillus oryzae. Biochem Biophys Res Commun. 1969 Oct 22;37(3):470–476. doi: 10.1016/0006-291x(69)90939-5. [DOI] [PubMed] [Google Scholar]
  195. Stevens L., Stevens E. Neutral proteinases in germinating conidia and hyphae of Aspergillus nidulans. Biochem Soc Trans. 1980 Oct;8(5):542–543. doi: 10.1042/bst0080542. [DOI] [PubMed] [Google Scholar]
  196. Subramanian E., Swan I. D., Liu M., Davies D. R., Jenkins J. A., Tickle I. J., Blundell T. L. Homology among acid proteases: comparison of crystal structures at 3A resolution of acid proteases from Rhizopus chinensis and Endothia parasitica. Proc Natl Acad Sci U S A. 1977 Feb;74(2):556–559. doi: 10.1073/pnas.74.2.556. [DOI] [PMC free article] [PubMed] [Google Scholar]
  197. Sugiura M., Suzuki M., Ishikawa M., Sasaki M. Pharmaceutical studies on aminopeptidase from Aspergillus japonica. Chem Pharm Bull (Tokyo) 1976 Oct;24(10):2286–2293. doi: 10.1248/cpb.24.2286. [DOI] [PubMed] [Google Scholar]
  198. Sun P. S., Chu F. S. Characterization of byssochlamyopeptidase A. Biochim Biophys Acta. 1979 May 10;568(1):91–102. doi: 10.1016/0005-2744(79)90276-6. [DOI] [PubMed] [Google Scholar]
  199. Suprynowicz F. A., Allewell N. M. Regulation of neutral protease activity through the life cycles of Tetrahymena pyriformis. Biochim Biophys Acta. 1979 Jul 18;585(4):488–498. doi: 10.1016/0304-4165(79)90182-x. [DOI] [PubMed] [Google Scholar]
  200. Switzer R. L. The inactivation of microbial enzymes in vivo. Annu Rev Microbiol. 1977;31:135–157. doi: 10.1146/annurev.mi.31.100177.001031. [DOI] [PubMed] [Google Scholar]
  201. Tanaka N., Takeuchi M., Ichishima E. Purification of an acid proteinase from Aspergillus saitoi and determination of peptide bond specificity. Biochim Biophys Acta. 1977 Dec 8;485(2):406–416. doi: 10.1016/0005-2744(77)90176-0. [DOI] [PubMed] [Google Scholar]
  202. Tang J. Evolution in the structure and function of carboxyl proteases. Mol Cell Biochem. 1979 Jul 31;26(2):93–109. doi: 10.1007/BF00232887. [DOI] [PubMed] [Google Scholar]
  203. Tang J., James M. N., Hsu I. N., Jenkins J. A., Blundell T. L. Structural evidence for gene duplication in the evolution of the acid proteases. Nature. 1978 Feb 16;271(5646):618–621. doi: 10.1038/271618a0. [DOI] [PubMed] [Google Scholar]
  204. Timberlake W. E., McDowell L., Cheney J., Griffin D. H. Protein synthesis during the differentiation of sporangia in the water mold Achlya. J Bacteriol. 1973 Oct;116(1):67–73. doi: 10.1128/jb.116.1.67-73.1973. [DOI] [PMC free article] [PubMed] [Google Scholar]
  205. Tortora P., Birtel M., Lenz A. G., Holzer H. Glucose-dependent metabolic interconversion of fructose-1, 6-bisphosphatase in yeast. Biochem Biophys Res Commun. 1981 May 29;100(2):688–695. doi: 10.1016/s0006-291x(81)80230-6. [DOI] [PubMed] [Google Scholar]
  206. Tsuchiya K., Kimura T. Production of trypsin inhibitor by a Cephalosporium sp. Appl Environ Microbiol. 1978 Apr;35(4):631–635. doi: 10.1128/aem.35.4.631-635.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  207. Tsujita Y., Endo A. Chemical properties of the polysaccharides associated with acid protease of Aspergillus oryzae grown on solid bran media. J Biochem. 1977 Apr;81(4):1063–1070. doi: 10.1093/oxfordjournals.jbchem.a131529. [DOI] [PubMed] [Google Scholar]
  208. Tsujita Y., Endo A. Intracellular localization of two molecular forms of membrane acid protease in Aspergillus oryzae. J Biochem. 1980 Jul;88(1):113–120. [PubMed] [Google Scholar]
  209. Tullis R. H., Rubin H. Calcium protects DNase I from proteinase K: a new method for the removal of contaminating RNase from DNase I. Anal Biochem. 1980 Sep 1;107(1):260–264. doi: 10.1016/0003-2697(80)90519-9. [DOI] [PubMed] [Google Scholar]
  210. Turkovã J., Mikes O., Hayashi K., Danno G., Polgãr L. Alkaline proteinases of the genus Aspergillus. Biochim Biophys Acta. 1972 Feb 29;257(2):257–263. doi: 10.1016/0005-2795(72)90277-2. [DOI] [PubMed] [Google Scholar]
  211. Tökés Z. A., Chambers S. M. Proteolytic activity associated with human erythrocyte membranes. Self-digestion of isolated human erythrocyte membranes. Biochim Biophys Acta. 1975 May 6;389(2):325–338. doi: 10.1016/0005-2736(75)90325-9. [DOI] [PubMed] [Google Scholar]
  212. VISWANATHA T., LIENER I. E. Isolation and properties of a proteinase from Tetrahymena pyriformis W. Arch Biochem Biophys. 1956 Apr;61(2):410–421. doi: 10.1016/0003-9861(56)90364-2. [DOI] [PubMed] [Google Scholar]
  213. VORBECK M. L., CONE J. F. Characteristics of an intracellullar proteinase system of a Trichosporon species isolated from Trappist-type cheese. Appl Microbiol. 1963 Jan;11:23–27. doi: 10.1128/am.11.1.23-27.1963. [DOI] [PMC free article] [PubMed] [Google Scholar]
  214. Venkatesan S., Bird R. G., Ormerod W. E. Intracellular enzymes and their localization in slender and stumpy forms of Trypanosoma brucei rhodesiense. Int J Parasitol. 1977 Apr;7(2):139–147. doi: 10.1016/0020-7519(77)90082-0. [DOI] [PubMed] [Google Scholar]
  215. Wang H. L. Release of proteinase from mycelium of Mucor hiemalis. J Bacteriol. 1967 Jun;93(6):1794–1799. doi: 10.1128/jb.93.6.1794-1799.1967. [DOI] [PMC free article] [PubMed] [Google Scholar]
  216. Wang H. L., Vespa J. B., Hesseltine C. W. Acid protease production by fungi used in soybean food fermentation. Appl Microbiol. 1974 May;27(5):906–911. doi: 10.1128/am.27.5.906-911.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  217. Wolf D. H. Control of metabolism in yeast and other lower eukaryotes through action of proteinases. Adv Microb Physiol. 1980;21:267–338. doi: 10.1016/s0065-2911(08)60358-6. [DOI] [PubMed] [Google Scholar]
  218. Wolf D. H., Ehmann C. Carboxypeptidase S- and carboxypeptidase Y-deficient mutants of Saccharomyces cerevisiae. J Bacteriol. 1981 Aug;147(2):418–426. doi: 10.1128/jb.147.2.418-426.1981. [DOI] [PMC free article] [PubMed] [Google Scholar]
  219. Wolf D. H., Ehmann C. Studies on a proteinase B mutant of yeast. Eur J Biochem. 1979 Aug 1;98(2):375–384. doi: 10.1111/j.1432-1033.1979.tb13197.x. [DOI] [PubMed] [Google Scholar]
  220. Wolf D. H., Fink G. R. Proteinase C (carboxypeptidase Y) mutant of yeast. J Bacteriol. 1975 Sep;123(3):1150–1156. doi: 10.1128/jb.123.3.1150-1156.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  221. Wolf D. H., Weiser U. Studies on a carboxypeptidase Y mutant of yeast and evidence for a second carboxypeptidase Activity. Eur J Biochem. 1977 Mar 1;73(2):553–556. doi: 10.1111/j.1432-1033.1977.tb11350.x. [DOI] [PubMed] [Google Scholar]
  222. Wright I. G., Goodger B. V., Mahoney D. F. Virulent and avirulent strains of Babesia bovis: The relationship between parasite protease content and pathophysiological effect on the strain. J Protozool. 1981 Feb;28(1):118–120. doi: 10.1111/j.1550-7408.1981.tb02815.x. [DOI] [PubMed] [Google Scholar]
  223. Wright I. G., Goodger B. V. Proteolytic enzyme activity in the intra-erythrocytic parasites Babesia argentina and Babesia bigemina. Z Parasitenkd. 1973 Oct 26;42(3):213–220. [PubMed] [Google Scholar]
  224. Yu R. J., Harmon S. R., Blank F. Hair digestion by a keratinase of Trichophyton mentagrophytes. J Invest Dermatol. 1969 Aug;53(2):166–171. [PubMed] [Google Scholar]
  225. Yu R. J., Harmon S. R., Grappel S. F., Blank F. Two cell-bound keratinases of Trichophyton mentagrophytes. J Invest Dermatol. 1971 Jan;56(1):27–32. doi: 10.1111/1523-1747.ep12291869. [DOI] [PubMed] [Google Scholar]
  226. Zdanowski M. K., Rasmussen L. Peptidase activity in Tetrahymena. J Cell Physiol. 1979 Sep;100(3):407–411. doi: 10.1002/jcp.1041000304. [DOI] [PubMed] [Google Scholar]
  227. Zeldin M. H., Skea W., Matteson D. Organelle formation in the presence of a protease inhibitor. Biochem Biophys Res Commun. 1973 May 15;52(2):544–549. doi: 10.1016/0006-291x(73)90746-8. [DOI] [PubMed] [Google Scholar]
  228. Zubenko G. S., Jones E. W. Catabolite inactivation of gluconeogenic enzymes in mutants of yeast deficient in proteinase B. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4581–4585. doi: 10.1073/pnas.76.9.4581. [DOI] [PMC free article] [PubMed] [Google Scholar]
  229. Zubenko G. S., Jones E. W. Protein degradation, meiosis and sporulation in proteinase-deficient mutants of Saccharomyces cerevisiae. Genetics. 1981 Jan;97(1):45–64. doi: 10.1093/genetics/97.1.45. [DOI] [PMC free article] [PubMed] [Google Scholar]
  230. Zubenko G. S., Mitchell A. P., Jones E. W. Mapping of the proteinase b structural gene PRB1, in Saccharomyces cerevisiae and identification of nonsense alleles within the locus. Genetics. 1980 Sep;96(1):137–146. doi: 10.1093/genetics/96.1.137. [DOI] [PMC free article] [PubMed] [Google Scholar]
  231. Zubenko G. S., Mitchell A. P., Jones E. W. Septum formation, cell division, and sporulation in mutants of yeast deficient in proteinase B. Proc Natl Acad Sci U S A. 1979 May;76(5):2395–2399. doi: 10.1073/pnas.76.5.2395. [DOI] [PMC free article] [PubMed] [Google Scholar]

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