Document Detail

Kinetics and thermodynamics of the slow hydrophobic deactivation of alpha-chymotrypsin.
MedLine Citation:
PMID:  1197384     Owner:  NLM     Status:  MEDLINE    
A quantitative model for the slow reversible hydrophobic deactivation of alpha-chymotrypsin (alpha-CT) is proposed. Kinetic results are obtained for (1) the situation in which the inhibitor concentration, although remaining constant during the course of a run, can be varied independently of the concentration of nonself-inhibiting substrate, and for (2) the situation in which the self-inhibiting substrate concentration decreases during the course of a run, and independent variation of inhibitor and substrate concentrations is not possible. Excellent quantitative agreement between theory and experiment is obtained for a wide range of conditions using 3-(n-hexanoyl-O-benzoate (with dodecylsulfate as the inhibitor), and 3-(n-decanoyl)-O-benzoate as the self-inhibiting substrate. Activation enthalpies and entropies for the hydrophobic deactivation of alpha-CT by dodecylsulfate and tetradecyltrimethylammonium are determined. For comparison, activation enthalpies and entropies for the alpha-CT hydrolysis of 3-(n-heptanoyl)-O-benzoate are determined; evidence for a thermally induced conformational transition in alpha-CT at 30 degrees C is obtained.
R N Smith; T P Poindexter; C Hansch
Related Documents :
21193014 - Possible involvement of calpain-like activity in normal processing of cellular prion pr...
19682254 - Esx-1 secreted virulence factors are recognized by multiple cytosolic aaa atpases in pa...
18601104 - Extractive bioconversions in aqueous two-phase systems: enzymatic hydrolysis of casein ...
1197384 - Kinetics and thermodynamics of the slow hydrophobic deactivation of alpha-chymotrypsin.
20217464 - Intramolecular charge transfer effects on flutamide drug.
2441724 - Horse alpha 2-macroglobulin. circular dichroism studies of conformational changes upon ...
Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Physiological chemistry and physics     Volume:  7     ISSN:  0031-9325     ISO Abbreviation:  Physiol. Chem. Phys.     Publication Date:  1975  
Date Detail:
Created Date:  1976-02-26     Completed Date:  1976-02-26     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  0202364     Medline TA:  Physiol Chem Phys     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  423-36     Citation Subset:  IM    
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Binding Sites
Chymotrypsin* / antagonists & inhibitors
Protein Binding
Structure-Activity Relationship
Reg. No./Substance:
0/Benzoates; EC

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

Previous Document:  The mechanism for the exclusion of sugars from the water in a model of the liveing cell: the ion-exc...
Next Document:  The effect of the presence of the metal prosthetic groups on the subunit structure of bovine superox...