Skip to main content
Infection and Immunity logoLink to Infection and Immunity
. 1981 Sep;33(3):738–742. doi: 10.1128/iai.33.3.738-742.1981

Isolation and characterization of proteases from Bacteroides melaninogenicus.

S Fujimura, T Nakamura
PMCID: PMC350771  PMID: 6116674

Abstract

We isolated two types of intracellular proteases from a strain of Bacteroides melaninogenicus. These enzymes were extracted from cells by ultrasonic treatment and were partially purified. These two enzymes (proteases I and II) differed in molecular weight, heat stability, sensitivity to reducing agents, Km value, and optimum pH for activity.

Full text

PDF
738

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Andrews P. Estimation of the molecular weights of proteins by Sephadex gel-filtration. Biochem J. 1964 May;91(2):222–233. doi: 10.1042/bj0910222. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Arvidson S., Holme T., Lindholm B. Studies on extracellular proteolytic enzymes from Staphylococcus aureus. I. Purification and characterization of one neutral and one alkaline protease. Biochim Biophys Acta. 1973 Mar 15;302(1):135–148. doi: 10.1016/0005-2744(73)90016-8. [DOI] [PubMed] [Google Scholar]
  3. Arvidson S. Studies on extracellular proteolytic enzymes from Staphylococcus aureus. II. Isolation and characterization of an EDTA-sensitive protease. Biochim Biophys Acta. 1973 Mar 15;302(1):149–157. doi: 10.1016/0005-2744(73)90017-x. [DOI] [PubMed] [Google Scholar]
  4. Balke E., Scharmann W. Untersuchungen an einer Protease (Elastase) aus Pseudomonas aeruginosa, II: Charakterisierung des Enzyms. Hoppe Seylers Z Physiol Chem. 1974 Aug;355(8):958–968. [PubMed] [Google Scholar]
  5. Boethling R. S. Purification and properties of a serine protease from Pseudomonas matophilia. J Bacteriol. 1975 Mar;121(3):933–941. doi: 10.1128/jb.121.3.933-941.1975. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Cheng Y. S., Zipser D., Cheng C. Y., Rolseth S. J. Isolation and characterization of mutations in the structural gene for protease III (ptr). J Bacteriol. 1979 Oct;140(1):125–130. doi: 10.1128/jb.140.1.125-130.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Cheng Y. S., Zipser D. Purification and characterization of protease III from Escherichia coli. J Biol Chem. 1979 Jun 10;254(11):4698–4706. [PubMed] [Google Scholar]
  8. Drapeau G. R., Boily Y., Houmard J. Purification and properties of an extracellular protease of Staphylococcus aureus. J Biol Chem. 1972 Oct 25;247(20):6720–6726. [PubMed] [Google Scholar]
  9. Fujimura S., Makino T., Hayashi T. T. Occurrence of a complex form of staphylokinase in the course of cultivation of Staphylococcus aureus. Appl Microbiol. 1974 Jul;28(1):5–10. doi: 10.1128/am.28.1.5-10.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Fujimura S., Nakamura T. Purification and properties of a bacteriocin-like substance (acnecin) of oral Propionibacterium acnes. Antimicrob Agents Chemother. 1978 Dec;14(6):893–898. doi: 10.1128/aac.14.6.893. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Fujimura S., Nakamura T. Sanguicin, a bacteriocin of oral Streptococcus sanguis. Antimicrob Agents Chemother. 1979 Sep;16(3):262–265. doi: 10.1128/aac.16.3.262. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Goldberg A. L. Correlation between rates of degradation of bacterial proteins in vivo and their sensitivity to proteases. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2640–2644. doi: 10.1073/pnas.69.9.2640. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Keay L., Feder J., Garrett L. R., Moseley M. H., Cirulis N. Bacillus megaterium neutral protease, a zinc-containing metalloenzyme. Biochim Biophys Acta. 1971 Mar 23;229(3):829–835. doi: 10.1016/0005-2795(71)90302-3. [DOI] [PubMed] [Google Scholar]
  14. Kreger A. S., Griffin O. K. Physicochemical fractionation of extracellular cornea-damaging proteases of Pseudomonas aeruginosa. Infect Immun. 1974 May;9(5):828–834. doi: 10.1128/iai.9.5.828-834.1974. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  16. Lyerly D., Kreger A. Purification and characterization of a Serratia marcescens metalloprotease. Infect Immun. 1979 May;24(2):411–421. doi: 10.1128/iai.24.2.411-421.1979. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Pacaud M. Purification of protease II from Escherichia coli by affinity chromatography and separation of two enzyme species from cells harvested at late log phase. Eur J Biochem. 1976 Apr 15;64(1):199–204. doi: 10.1111/j.1432-1033.1976.tb10288.x. [DOI] [PubMed] [Google Scholar]
  18. Pacaud M., Richaud C. Protease II from Escherichia coli. Purification and characterization. J Biol Chem. 1975 Oct 10;250(19):7771–7779. [PubMed] [Google Scholar]
  19. Pacaud M., Sibilli S., Bras G. Protease I from Escherichia coli. Some physicochemical properties and substrate specificity. Eur J Biochem. 1976 Oct 1;69(1):141–151. doi: 10.1111/j.1432-1033.1976.tb10867.x. [DOI] [PubMed] [Google Scholar]
  20. Pacaud M., Uriel J. Isolation and some propeties of a proteolytic enzyme from Escherichia coli (protease I). Eur J Biochem. 1971 Dec 10;23(3):435–442. doi: 10.1111/j.1432-1033.1971.tb01638.x. [DOI] [PubMed] [Google Scholar]
  21. Porzio M. A., Pearson A. M. Isolation of an extracellular neutral proteinase from Pseudomonas fragi. Biochim Biophys Acta. 1975 Mar 28;384(1):235–241. doi: 10.1016/0005-2744(75)90112-6. [DOI] [PubMed] [Google Scholar]
  22. Pulverer G., Ko H. L., Wegrzynowicz Z., Jeljaszewicz J. Clotting and fibrinolytic activities of Bacteroides melaninogenicus. Zentralbl Bakteriol Orig A. 1977 Dec;239(4):510–513. [PubMed] [Google Scholar]
  23. Stepanov V. M., Strongin A. Y., Izotova L. S., Abramov Z. T., Lyublinskaya L. A., Ermakova L. M., Baratova L. A., Belyanova L. P. Intracellular serine protease from Bacillus subtilis. Structural comparison with extracellular serine proteases-subtilisins. Biochem Biophys Res Commun. 1977 Jul 11;77(1):298–305. doi: 10.1016/s0006-291x(77)80196-4. [DOI] [PubMed] [Google Scholar]
  24. Strongin A. Y., Gorodetsky D. I., Stepanov V. M. The study of Escherichia coli proteases. Intracellular serine protease of E. coli-an analogue of bacillus proteases. J Gen Microbiol. 1979 Feb;110(2):443–451. doi: 10.1099/00221287-110-2-443. [DOI] [PubMed] [Google Scholar]
  25. Strongin A. Y., Izotova L. S., Abramov Z. T., Gorodetsky D. I., Ermakova L. M., Baratova L. A., Belyanova L. P., Stepanov V. M. Intracellular serine protease of Bacillus subtilis: sequence homology with extracellular subtilisins. J Bacteriol. 1978 Mar;133(3):1401–1411. doi: 10.1128/jb.133.3.1401-1411.1978. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. Wegrzynowicz Z., Ko H. J., Pulverer G., Jeljaszewicz J. The nature of clotting and fibrinolytic activities of Bacteroids melaninogenicus. Zentralbl Bakteriol Orig A. 1978 Jan;240(1):106–111. [PubMed] [Google Scholar]
  27. Wretlind B., Wadström T. Purification and properties of a protease with elastase activity from Pseudomonas aeruginosa. J Gen Microbiol. 1977 Dec;103(2):319–327. doi: 10.1099/00221287-103-2-319. [DOI] [PubMed] [Google Scholar]
  28. Yoshida E., Noda H. Isolation and characterization of collagenases I and II from Clostridium histolyticum. Biochim Biophys Acta. 1965 Sep 20;105(3):562–574. doi: 10.1016/s0926-6593(65)80239-9. [DOI] [PubMed] [Google Scholar]

Articles from Infection and Immunity are provided here courtesy of American Society for Microbiology (ASM)

RESOURCES