Kinetics of the Reaction of α-Chymotrypsin with Diisopropyl Fluorophosphate, with Measurements of Hydrogen Ion Release, Enzyme Inhibition, and Spectral Changes of Enzyme at 290 mµ-Reference-Cited by-同舟云学术

Kinetics of the Reaction of α-Chymotrypsin with Diisopropyl Fluorophosphate, with Measurements of Hydrogen Ion Release, Enzyme Inhibition, and Spectral Changes of Enzyme at 290 mµ

Published:1965-11 Issue:11 Volume:240 Page:4204-4212
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Moon A. Young,Sturtevant Julian M.,Hess George P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference41 articles.

1. Conformational Changes Accompanying An Enzyme Catalyzed Reaction

2. CONFORMATIONAL CHANGES IN ENZYME CATALYSIS

3. Evidence for Conformational Changes in α-Chymotrypsin Catalyzed Reactions. VII. Thermal Induced Reversible Changes of Conformation at pH 2.0

4. Interpretation of the ultraviolet spectrum of trans-cinnamoyl-α-chymotrypsin

5. Substrate Control of Conformation Characteristics in Chymotrypsin

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