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• W1976895606 abstract "Abstract— Angiotensin converting enzyme (peptidyl dipeptide hydrolase EC 3.4.15.1) was extracted from particulates of rat brain using the nonionic detergent Triton X-100. Enzyme activity in subcellular fractions was associated with purified synaptosomes and present in the microsomal fraction, but absent in purified mitochondria and water-shocked myelin. Partial purification was achieved by chromatography on DEAE-cellulose and hydroxylapatite columns. The enzyme had a pH optimum of pH 7–8 and an apparent Km of 2.2 mm using hippuryl-histidyl-leucine as substrate; it was chloride dependent, inhibited by (Sar1-Ala8)-angiotensin-II (saralasin), and, at lower concentrations, by the specific nonapeptide inhibitor SQ 20881. Associated with the purified enzyme was an aminopeptidase, cleaving N-terminal Asp from the native substrate, which could be involved in the production of the active heptapeptide, angiotensin III (des-Asp-angiotensin-II). Also present was a carboxypeptidase-like enzyme removing C-terminal Phe following the liberation of His-Leu by converting enzyme, which may be involved in the inactivation of angiotensin II or III." @default.
• W1976895606 created "2016-06-24" @default.
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• W1976895606 date "1978-04-01" @default.
• W1976895606 modified "2023-10-18" @default.
• W1976895606 title "SUBCELLULAR LOCALIZATION AND PARTIAL PURIFICATION OF A CHLORIDE DEPENDENT ANGIOTENSIN-I CONVERTING ENZYME FROM RAT BRAIN" @default.
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• W1976895606 doi "https://doi.org/10.1111/j.1471-4159.1978.tb10778.x" @default.
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