Literature DB >> 426776

Activation of cathepsin D by glycine ethyl ester.

A Dionyssiou-Asteriou, E T Rakitzis.   

Abstract

Cathepsin D purified from bovine spleen is activated by glycine ethyl ester. A maximum of 70% activation was observed at a glycine ethyl ester concentration of 0.1 M and at pH 4.5. The activation effect appears to be reversible.

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Year:  1979        PMID： 426776      PMCID： PMC1186374          DOI： 10.1042/bj1770355

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  4 in total

1.  Inactivation of cathepsin D by dithiophosgene and by 2,2-dichloro-1,3-dithiacyclobutanone.

Authors:  E T Rakitzis; T B Malliopoulou
Journal:  Biochem J       Date:  1976-03-01       Impact factor: 3.857

2.  The effect of urea upon the activity measurement of cod muscle cathepsin with hemoglobin substrate.

Authors:  M B Wojtowicz; P Odense
Journal:  Can J Biochem       Date:  1970-09

3.  Kinetics of irreversible enzyme inhibition by an unstable inhibitor.

Authors:  E T Rakitzis
Journal:  Biochem J       Date:  1974-08       Impact factor: 3.857

4.  Inactivation of cathepsin D from human gastric mucosa and from stomach carcinoma by diazoacetyl-DL-norleucine methyl ester.

Authors:  A Dionyssiou-Asteriou; E T Rakitzis
Journal:  Biochem Pharmacol       Date:  1978-03-01       Impact factor: 5.858
  4 in total
  1 in total

1.  The kinetics of hydrolysis of some synthetic substrates containing neutral hydrophilic groups by pig pepsin and chicken liver cathepsin D.

Authors:  G B Irvine; N L Blumsom; D T Elmore
Journal:  Biochem J       Date:  1983-04-01       Impact factor: 3.857
  1 in total

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