Document Detail


Partial characterization of angiotensin I-converting enzyme of the aorta in rats.
MedLine Citation:
PMID:  6088824     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The angiotensin I-converting enzyme of rat aorta was solubilized with Triton X-100 and partially purified by chromatography with DEAE-cellulose and Sephadex G-200. The specific activity of the purified enzyme was 4.01 units/mg of protein. The enzyme was separated into 6 isozymes with different molecular weights of 460,000, 440,000, 260,000, 220,000, 217,000 and 119,000 by Sephadex G-200 gel filtration. All the isozymes migrated as a single band with a molecular weight of 112,000 on SDS/polyacrylamide gel electrophoresis. These isozymes showed the same optimal pH (8.3) and temperature (30 degrees C). Converting-enzyme, which might be produced in the arterial wall, may play a role in the local control of vascular tone through the conversion of angiotensin I into II in vascular tissue.
Authors:
K Mizuno; S Fukuchi; A Kimura
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Japanese heart journal     Volume:  25     ISSN:  0021-4868     ISO Abbreviation:  Jpn Heart J     Publication Date:  1984 May 
Date Detail:
Created Date:  1984-10-23     Completed Date:  1984-10-23     Revised Date:  2003-11-14    
Medline Journal Info:
Nlm Unique ID:  0401175     Medline TA:  Jpn Heart J     Country:  JAPAN    
Other Details:
Languages:  eng     Pagination:  387-96     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Animals
Aorta / enzymology*
Chromatography, DEAE-Cellulose
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Male
Molecular Weight
Peptidyl-Dipeptidase A* / isolation & purification
Rats
Rats, Inbred Strains
Chemical
Reg. No./Substance:
EC 3.4.15.1/Peptidyl-Dipeptidase A

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


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