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Literature DB >> 43135

A radiochemical titrant for the determination of the operational molarity of solutions of acid proteinases.

Abstract

N-Diazoacetyl-L-phenylalanine 3-phenyl[2,3-3H]propylamide was synthesized and shown to inhibit pepsin A (EC3,4,23.1) and cathepsin D (EC 3.4.23.5) irreversibly and stoicheiometrically in the presence of Cu2+. Quantitative separation of the inhibited enzyme from excess reagent by gel filtration followed by measurement of the radioactivity of the protein peak provided a method for determining the operational molarity of these enzymes. Several other putative active-site-directed irreversible inhibitors were synthesized, but were inactive. Data on the synthesis of these compounds have been deposited as Supplementary Publication SUP50096 (4 pages) at the British Library Lending Division, Boston Spa, Wetherby, West Yorkshire LS23 7BQ, U.K., from whom copies can be obtained on the terms indicated in Biochem. J. (1978) 169, 5.

Entities: Chemical Gene

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Year: 1979 PMID： 43135 PMCID： PMC1161570 DOI： 10.1042/bj1830389

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

12 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

2. Inactivation of aspartyl proteinases by butane-2,3-dione. Modification of tryptophan and tyrosine residues and evidence against reaction of arginine residues.

Authors: J C Gripon; T Hofmann
Journal: Biochem J Date: 1981-01-01 Impact factor: 3.857

2 in total

A radiochemical titrant for the determination of the operational molarity of solutions of acid proteinases.

1. Inhibition of cathepsin D by diazoacetylnorleucine methyl ester.

2. EFFECT OF SOLVENTS AND OF TEMPERATURE ON THE OPTICAL ROTATORY PROPERTIES OF PEPSIN.

3. Effect of cathepsins D from normal and malignant tissues on synthetic peptides.

4. A filter assay for thymidylate synthetase using 5-fluoro-2'-deoxyuridylate as an active site titrant.

5. On the reaction of diazoacetyl compounds with pepsin.

6. An aspartic acid residue at the active site of pepsin. The isolation and sequence of the heptapeptide.

7. The inactivation of pepsin by diazoacetylnorleucine methyl ester.

8. The use of a radiochemical titrant for the determination of the operational molarity of solutions of pepsin.

9. Bifunctional inhibitors of pepsin.

10. Cathepsin D. Purification of isoenzymes from human and chicken liver.

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

2. Inactivation of aspartyl proteinases by butane-2,3-dione. Modification of tryptophan and tyrosine residues and evidence against reaction of arginine residues.