Document Detail


A chemical relaxation study of human prostatic acid phosphatase.
MedLine Citation:
PMID:  5641399     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Chemical relaxation methods and a dilution technique were applied to the study of the hydrolysis of p-nitrophenyl phosphate by human prostatic acid phosphatase. Although the reaction mechanism was not elucidated, rate constants and equilibrium constants were obtained for the reaction of enzyme and p-nitrophenol to form a complex. A slow, 2-sec relaxation effect which showed no concentration dependence was observed in various reaction mixtures, including some lacking the substrate and products of the hydrolytic reaction. The conclusion drawn is that there are two forms of the prostatic enzyme, which are normally in equilibrium with each other, but which undergo a relatively slow interconversion when this equilibrium is perturbed. A preliminary calculation indicates that these forms are present in the equilibrium ratio of 2:1.
Authors:
D B Shear; K Kustin
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biophysical journal     Volume:  8     ISSN:  0006-3495     ISO Abbreviation:  Biophys. J.     Publication Date:  1968 Jan 
Date Detail:
Created Date:  1968-05-09     Completed Date:  1968-05-09     Revised Date:  2010-09-13    
Medline Journal Info:
Nlm Unique ID:  0370626     Medline TA:  Biophys J     Country:  UNITED STATES    
Other Details:
Languages:  eng     Pagination:  139-43     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Acid Phosphatase / metabolism*
Humans
Isoenzymes
Kinetics
Male
Mathematics
Progesterone / analysis
Prostate / enzymology*
Temperature
Chemical
Reg. No./Substance:
0/Isoenzymes; 57-83-0/Progesterone; EC 3.1.3.2/Acid Phosphatase
Comments/Corrections

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


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