Document Detail


Characterization of an intracellular inhibitor of the carboxypeptidase R from Rhodotorula glutinis.
MedLine Citation:
PMID:  573739     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
A peptidic inhibitor of the carboxypeptidase R from Rhodotorula glutinis has been identified and partially purified. A molecular weight of 31 000 was found by gel filtration. The inhibitor is reversibly separated from the carboxypeptidase by chaotropic agents. Removal of the inhibitor by an acid protease explains the osberved activation of the carboxypeptidase by incubation at acidic pH values.
Authors:
M Hernández-Jodra; C Gancedo
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Hoppe-Seyler's Zeitschrift für physiologische Chemie     Volume:  360     ISSN:  0018-4888     ISO Abbreviation:  Hoppe-Seyler's Z. Physiol. Chem.     Publication Date:  1979 Jul 
Date Detail:
Created Date:  1979-12-20     Completed Date:  1979-12-20     Revised Date:  2000-12-18    
Medline Journal Info:
Nlm Unique ID:  2985060R     Medline TA:  Hoppe Seylers Z Physiol Chem     Country:  GERMANY, WEST    
Other Details:
Languages:  eng     Pagination:  913-7     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Carboxypeptidases / antagonists & inhibitors*
Guanidines / pharmacology
Kinetics
Mitosporic Fungi / enzymology*
Molecular Weight
Peptides / isolation & purification,  physiology*
Rhodotorula / enzymology*
Thiocyanates / pharmacology
Chemical
Reg. No./Substance:
0/Guanidines; 0/Peptides; 0/Thiocyanates; EC 3.4.-/Carboxypeptidases

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


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