Document Detail


Purification and partial characterization of rat brain acid proteinase (isorenin).
MedLine Citation:
PMID:  23850     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
1. Isorenin was purified 2000-fold from rat brain by a simple 3-step procedure involving affinity chromatography on pepstatinyl-Sepharose, The preparation appears as a homogenous protein in analytical polyacrylamide gel electrophoresis. Sodium dodecyl sulfate gel electrophoresis indicated an apparent molecular weight of 45 000. Isoelectric focusing separated isoenzymes with isoelectric points at pH 5.45, 5.87, 6.16 and 7.05. 2. The enzyme generates antiotensin I from tetradecapeptide (pH optimum 4.7) and from sheep angiotensinogen (pH optima 3.9 and 5.5). The rate of angiotensin I formation from tetradecapeptide was 30 000 times higher than that from sheep angiotensinogen. The enzyme has acid protease activity at pH 3.2 with hemoglobin as the substrate and pepstatin is a potent inhibitor of the enzyme with a Ki of less than 10(-9) M. 3. The properties of the enzyme strongly suggest that it is identical with cathepsin D.
Authors:
E Hackenthal; R Hackenthal; U Hilgenfeldt
Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  522     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1978 Feb 
Date Detail:
Created Date:  1978-04-17     Completed Date:  1978-04-17     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  561-73     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Angiotensin I / biosynthesis
Angiotensinogen / metabolism
Animals
Brain / enzymology*
Endopeptidases / isolation & purification,  metabolism*
Hydrogen-Ion Concentration
Male
Molecular Weight
Pepstatins / pharmacology
Rats
Chemical
Reg. No./Substance:
0/Pepstatins; 11002-13-4/Angiotensinogen; 9041-90-1/Angiotensin I; EC 3.4.-/Endopeptidases

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


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