Skip to main content
Biochemical Journal logoLink to Biochemical Journal
. 1961 Feb;78(2):418–424. doi: 10.1042/bj0780418

Tissue-specific and species-specific esterases

J Paul 1, P Fottrell 1
PMCID: PMC1205284  PMID: 13733434

Full text

PDF
419

Images in this article

Selected References

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

  1. AUGUSTINSSON K. B. Electrophoretic separation and classification of blood plasma esterases. Nature. 1958 Jun 28;181(4626):1786–1789. doi: 10.1038/1811786a0. [DOI] [PubMed] [Google Scholar]
  2. COHEN J. A., JANSZ H. S., OOSTERBAAN R. A. The chemical structure of the reactive group of esterases. Biochim Biophys Acta. 1956 May;20(2):402–403. doi: 10.1016/0006-3002(56)90310-9. [DOI] [PubMed] [Google Scholar]
  3. FULTON W. C., LESLIE I., SINCLAIR R. Biochemical tests for malignancy applied to a new strain of human cells. Nature. 1956 Nov 24;178(4543):1179–1180. doi: 10.1038/1781179a0. [DOI] [PubMed] [Google Scholar]
  4. HARRIS J. I., LI C. H. Corticotropins (ACTH). IV. The action of carboxypeptidase on alpha-corticotropin, and the C-terminal amino acid sequence. J Biol Chem. 1955 Apr;213(2):499–507. [PubMed] [Google Scholar]
  5. HENION W. F., SUTHERLAND E. W. Immunological differences of phosphorylases. J Biol Chem. 1957 Jan;224(1):477–488. [PubMed] [Google Scholar]
  6. HILL R. L., SMITH E. L. Hydrolysis of mercuripapain by leucine aminopeptidase without loss of enzymic activity. J Biol Chem. 1958 Mar;231(1):117–134. [PubMed] [Google Scholar]
  7. HIRS C. H. W., MOORE S., STEIN W. H. A chromatographic investigation of pancreatic ribonuclease. J Biol Chem. 1953 Feb;200(2):493–506. [PubMed] [Google Scholar]
  8. HUNTER R. L., MARKERT C. L. Histochemical demonstration of enzymes separated by zone electrophoresis in starch gels. Science. 1957 Jun 28;125(3261):1294–1295. doi: 10.1126/science.125.3261.1294-a. [DOI] [PubMed] [Google Scholar]
  9. KREBS E. G. Yeast Glyceraldehyde-3-phosphate dehydrogenase. I. Electrophoresis of fractions precipitated by nucleic acid. J Biol Chem. 1953 Feb;200(2):471–478. [PubMed] [Google Scholar]
  10. LATNER A. L., ZAKI A. H. Starch-gel electrophoresis of animal sera. Nature. 1957 Dec 14;180(4598):1366–1367. doi: 10.1038/1801366a0. [DOI] [PubMed] [Google Scholar]
  11. MALMSTROM B. G. The purification of yeast enolase by zone electrophoresis and ion-exchange chromatography, and the existence of several active forms of the enzyme. Arch Biochem Biophys. 1957 Jul;70(1):58–69. doi: 10.1016/0003-9861(57)90080-2. [DOI] [PubMed] [Google Scholar]
  12. MEISTER A. Reduction of alpha gamma-diketo and alpha-keto acids catalyzed by muscle preparations and by crystalline lactic dehydrogenase. J Biol Chem. 1950 May;184(1):117–129. [PubMed] [Google Scholar]
  13. MILLS G. T., PAUL J., SMITH E. E. B. Studies on beta-glucuronidase. II. The preparation and properties of three-ox-spleen beta-glucuronidase fractions. Biochem J. 1953 Jan;53(2):232–245. doi: 10.1042/bj0530232. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Markert C. L., Møller F. MULTIPLE FORMS OF ENZYMES: TISSUE, ONTOGENETIC, AND SPECIES SPECIFIC PATTERNS. Proc Natl Acad Sci U S A. 1959 May;45(5):753–763. doi: 10.1073/pnas.45.5.753. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. NEILANDS J. B. Studies on lactic dehydrogenase of heart. I. Purity, kinetics, and equilibria. J Biol Chem. 1952 Nov;199(1):373–381. [PubMed] [Google Scholar]
  16. NISSELBAUM J. S., BODANSKY O. Reactions of lactic dehydrogenase from various rabbit organs with antirabbit muscle lactic dehydrogenase. J Biol Chem. 1959 Dec;234:3276–3280. [PubMed] [Google Scholar]
  17. OOSTERBAAN R. A., KUNST P., VAN ROTTERDAM J., COHEN J. A. The reaction of chymotrypsin and diisopropylphosphorofluoridate. I. Isolation and analysis of diisopropylphosphoryl-peptides. Biochim Biophys Acta. 1958 Mar;27(3):549–555. doi: 10.1016/0006-3002(58)90385-8. [DOI] [PubMed] [Google Scholar]
  18. PEDERSEN K. O. Size relationship among similar proteins; association and dissociation reactions of protein units. Cold Spring Harb Symp Quant Biol. 1950;14:140–152. doi: 10.1101/sqb.1950.014.01.018. [DOI] [PubMed] [Google Scholar]
  19. PERLMANN G. E. Formation of enzymatically active, dialysable fragments during autodigestion of pepsin. Nature. 1954 Feb 27;173(4400):406–406. doi: 10.1038/173406a0. [DOI] [PubMed] [Google Scholar]
  20. PORTER G. R., RYDON H. N., SCHOFIELD J. A. Nature of the reactive serine residue in enzymes inhibited by organo-phosphorus compounds. Nature. 1958 Oct 4;182(4640):927–927. doi: 10.1038/182927a0. [DOI] [PubMed] [Google Scholar]
  21. POULIK M. D. Starch gel electrophoresis in a discontinous system of buffers. Nature. 1957 Dec 28;180(4600):1477–1479. doi: 10.1038/1801477a0. [DOI] [PubMed] [Google Scholar]
  22. RICHARDS F. M. On an active intermediate produced during the digestion of ribonuclease by subtilisin. C R Trav Lab Carlsberg Chim. 1955;29(17-19):329–346. [PubMed] [Google Scholar]
  23. ROGERS W. I., KALNITSKY G. Partially hydrolyzed ribonuclease with enzymic activity. Biochim Biophys Acta. 1957 Mar;23(3):525–532. doi: 10.1016/0006-3002(57)90372-4. [DOI] [PubMed] [Google Scholar]
  24. SCHLAMOWITZ M. Immunochemical studies on alkaline phosphatase. Ann N Y Acad Sci. 1958 Oct 13;75(1):373–379. doi: 10.1111/j.1749-6632.1958.tb36885.x. [DOI] [PubMed] [Google Scholar]
  25. SMITHIES O. An improved procedure for starch-gel electrophoresis: further variations in the serum proteins of normal individuals. Biochem J. 1959 Mar;71(3):585–587. doi: 10.1042/bj0710585. [DOI] [PMC free article] [PubMed] [Google Scholar]
  26. SMITHIES O. Zone electrophoresis in starch gels: group variations in the serum proteins of normal human adults. Biochem J. 1955 Dec;61(4):629–641. doi: 10.1042/bj0610629. [DOI] [PMC free article] [PubMed] [Google Scholar]
  27. TALLAN H. H., STEIN W. H. Chromatographic studies on lysozyme. J Biol Chem. 1953 Feb;200(2):507–514. [PubMed] [Google Scholar]
  28. TIMASHEFF S. N., STURTEVANT J. M., BIER M. On the electrophoretic heterogeneity of trypsin. Arch Biochem Biophys. 1956 Jul;63(1):243–246. doi: 10.1016/0003-9861(56)90027-3. [DOI] [PubMed] [Google Scholar]
  29. TOOLAN H. W. Transplantable human neoplasms maintained in cortisone-treated laboratory animals: H.S. No. 1; H.Ep. No. 1; H.Ep. No. 2; H.Ep. No. 3; and H.Emb.Rh. No. 1. Cancer Res. 1954 Oct;14(9):660–666. [PubMed] [Google Scholar]

Articles from Biochemical Journal are provided here courtesy of The Biochemical Society

RESOURCES