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Literature DB >> 2176463

Effect of temperature and chloride on steady-state inhibition of angiotensin I-converting enzyme by enalaprilat and ramiprilat.

Abstract

The kinetics of the steady-state inhibition of angiotension I-converting enzyme (EC 3.4.15.1) at 25 degrees C and 37 degrees C with enalaprilat and ramiprilat can be simulated, assuming only one inhibitor-binding site, consistent with a 1:1 stoichiometry if the protein concentration was determined by amino acid analysis. In this temperature range the apparent inhibition constants for ramiprilat and enalaprilat were roughly doubled by a decrease in the chloride concentration from 0.300 M to 0.120 M.

Entities: Chemical

Mesh：

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Year: 1990 PMID： 2176463 PMCID： PMC1149715 DOI： 10.1042/bj2720415

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

28 in total

4. Steady-state enzyme kinetics with high-affinity substrates or inhibitors. A statistical treatment of dose-response curves.

Authors: P J Henderson
Journal: Biochem J Date: 1973-09 Impact factor: 3.857

5. Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models.

Authors: B Mannervik
Journal: Methods Enzymol Date: 1982 Impact factor: 1.600

Effect of temperature and chloride on steady-state inhibition of angiotensin I-converting enzyme by enalaprilat and ramiprilat.

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3. Protein measurement with the Folin phenol reagent.

4. Steady-state enzyme kinetics with high-affinity substrates or inhibitors. A statistical treatment of dose-response curves.

5. Regression analysis, experimental error, and statistical criteria in the design and analysis of experiments for discrimination between rival kinetic models.

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9. Kinetics of the reversible inhibition of enzyme-catalysed reactions by tight-binding inhibitors.

10. Molecular and catalytic properties of rabbit testicular dipeptidyl carboxypeptidase.

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