| Characterization of an intracellular inhibitor of the carboxypeptidase R from Rhodotorula glutinis. | |
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MedLine Citation:
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PMID: 573739 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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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. |
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Authors:
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M Hernández-Jodra; C Gancedo |
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Publication Detail:
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Type: Journal Article |
Journal Detail:
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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:
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Created Date: 1979-12-20 Completed Date: 1979-12-20 Revised Date: 2000-12-18 |
Medline Journal Info:
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Nlm Unique ID: 2985060R Medline TA: Hoppe Seylers Z Physiol Chem Country: GERMANY, WEST |
Other Details:
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Languages: eng Pagination: 913-7 Citation Subset: IM |
Export Citation:
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APA/MLA Format Download EndNote Download BibTex |
| MeSH Terms | |
Descriptor/Qualifier:
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Carboxypeptidases
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antagonists & inhibitors* Guanidines / pharmacology Kinetics Mitosporic Fungi / enzymology* Molecular Weight Peptides / isolation & purification, physiology* Rhodotorula / enzymology* Thiocyanates / pharmacology |
| Chemical | |
Reg. No./Substance:
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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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