Skip to main content
NCBI home page
Biochemical Journal logoLink to Biochemical Journal
. 1980 Jun 1;187(3):909–912. doi: 10.1042/bj1870909

Fluorimetric assays for cathepsin B and cathepsin H with methylcoumarylamide substrates.

A J Barrett
PMCID: PMC1162479  PMID: 6897924

Abstract

Benzyloxycarbonyl-phenylalanyl-arginine 4-methyl-7-coumarylamide was found to be an excellent substrate for the fluorimetric assay of cathepsin B, and arginine 4-methyl-7-coumarylamide for cathepsin H. Procedures were developed that are very convenient, and avoid the hazards associated with the use of naphthylamides.

Full text

PDF
909

Selected References

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

  1. Barrett A. J. A new assay for cathepsin B1 and other thiol proteinases. Anal Biochem. 1972 May;47(1):280–293. doi: 10.1016/0003-2697(72)90302-8. [DOI] [PubMed] [Google Scholar]
  2. Barrett A. J. An improved color reagent for use in Barrett's assay of Cathepsin B. Anal Biochem. 1976 Nov;76(50):374–376. doi: 10.1016/0003-2697(76)90298-0. [DOI] [PubMed] [Google Scholar]
  3. Barrett A. J. Human cathepsin B1. Purification and some properties of the enzyme. Biochem J. 1973 Apr;131(4):809–822. doi: 10.1042/bj1310809. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Barrett A. J., Poole A. R. Unsuitability of leucine naphthylamide for the histochemical demonstration of lysosomal proteolytic activity. Nature. 1969 Oct 18;224(5216):279–280. doi: 10.1038/224279a0. [DOI] [PubMed] [Google Scholar]
  5. Castillo M. J., Nakajima K., Zimmerman M., Powers J. C. Sensitive substrates for human leukocyte and porcine pancreatic elastase: a study of the merits of various chromophoric and fluorogenic leaving groups in assays for serine proteases. Anal Biochem. 1979 Oct 15;99(1):53–64. doi: 10.1016/0003-2697(79)90043-5. [DOI] [PubMed] [Google Scholar]
  6. Hardy M. F., Pennington R. J. Separation of cathepsin B1 and related enzymes from rat skeletal muscle. Biochim Biophys Acta. 1979 Apr 25;577(2):253–266. doi: 10.1016/0005-2795(79)90029-1. [DOI] [PubMed] [Google Scholar]
  7. Järvinen M., Hopsu-Havu V. K. alpha-N-benzoylarginine-2-naphthylamide hydrolase (cathepsin B1 ?) from rat skin. II. Purification of the enzyme and demonstration of two inhibitors in the skin. Acta Chem Scand B. 1975;29(7):772–780. doi: 10.3891/acta.chem.scand.29b-0772. [DOI] [PubMed] [Google Scholar]
  8. Kirschke H., Langner J., Wiederanders B., Ansorge S., Bohley P. Cathepsin L. A new proteinase from rat-liver lysosomes. Eur J Biochem. 1977 Apr 1;74(2):293–301. doi: 10.1111/j.1432-1033.1977.tb11393.x. [DOI] [PubMed] [Google Scholar]
  9. Kirschke H., Langner J., Wiederanders B., Ansorge S., Bohley P., Hanson H. Cathepsin H: an endoaminopeptidase from rat liver lysosomes. Acta Biol Med Ger. 1977;36(2):185–199. [PubMed] [Google Scholar]
  10. MacGregor R. R., Hamilton J. W., Shofstall R. E., Cohn D. V. Isolation and characterization of porcine parathyroid cathepsin B. J Biol Chem. 1979 Jun 10;254(11):4423–4427. [PubMed] [Google Scholar]
  11. McDonald J. K., Ellis S. On the substrate specificity of cathepsins B1 and B2 including a new fluorogenic substrate for cathepsin B1. Life Sci. 1975 Oct 15;17(8):1269–1276. doi: 10.1016/0024-3205(75)90137-x. [DOI] [PubMed] [Google Scholar]
  12. McDonald J. K., Zeitman B. B., Ellis S. Leucine naphthylamide: an inappropriate [corrected] substrate for the histochemical detection of cathepsins B and B'. Nature. 1970 Mar 14;225(5237):1048–1049. doi: 10.1038/2251048a0. [DOI] [PubMed] [Google Scholar]
  13. Morita T., Kato H., Iwanaga S., Takada K., Kimura T. New fluorogenic substrates for alpha-thrombin, factor Xa, kallikreins, and urokinase. J Biochem. 1977 Nov;82(5):1495–1498. doi: 10.1093/oxfordjournals.jbchem.a131840. [DOI] [PubMed] [Google Scholar]
  14. Schechter I., Berger A. On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain. Biochem Biophys Res Commun. 1968 Sep 6;32(5):898–902. doi: 10.1016/0006-291x(68)90326-4. [DOI] [PubMed] [Google Scholar]
  15. 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]
  16. Singh H., Kalnitsky G. Separation of a new alpha-N-benzoylarginine-beta-naphthylamide hydrolase from cathepsin B1. Purification, characterization, and properties of both enzymes from rabbit lung. J Biol Chem. 1978 Jun 25;253(12):4319–4326. [PubMed] [Google Scholar]
  17. WILKINSON G. N. Statistical estimations in enzyme kinetics. Biochem J. 1961 Aug;80:324–332. doi: 10.1042/bj0800324. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Watanabe H., Green G. D., Shaw E. A comparison of the behavior of chymotrypsin and cathepsin B towards peptidyl diazomethyl ketones. Biochem Biophys Res Commun. 1979 Aug 28;89(4):1354–1360. doi: 10.1016/0006-291x(79)92158-2. [DOI] [PubMed] [Google Scholar]

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

RESOURCES