AN AMINOPEPTIDASE ACTIVITY IN BOVINE PITUITARY SECRETORY VESICLES THAT CLEAVES THE N-TERMINAL ARGININE FROM BETA-LIPOTROPIN60-65
AN AMINOPEPTIDASE ACTIVITY IN BOVINE PITUITARY SECRETORY VESICLES THAT CLEAVES THE N-TERMINAL ARGININE FROM BETA-LIPOTROPIN60-65
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DOI：
10.1016/0014-5793(84)80586-4
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发表时间：
1984-01-01
期刊：
影响因子：
3.5
通讯作者：
LOH, YP
中科院分区：
文献类型：
--
作者：
GAINER, H;RUSSELL, JT;LOH, YP
Secretory vesicles isolated from the neural and intermediate lobes of the bovine pituitary contained a membrane-bound aminopeptidase activity which cleaved arginine from β-LPH60–65(Arg-Tyr-Gly-Gly-Phe-Met) and Arg-MCA. Neither methionine enkephalin (Tyr-Gly-Gly-Phe-Met) nor Substance P, which has an N-terminal arginine followed by a proline, could serve as substrates for this aminopeptidase activity; nor could cathepsin B-like or chymotrypsin-like enzyme activities be detected in the vesicle preparations. Maximal enzyme activity was at pH 6.0, and the activity was inhibited by EDTA, stimulated by Co2+and Zn2+, but was unaffected by leupeptin, pepstatin A, phenylmethylsulfonyl fluoride andp-chloromercuribenzenesulfonate, suggesting that the enzyme is a metalloaminopeptidase. The presence of this aminopeptidase activity in secretory vesicles suggests that it may be involved in peptide prohormone processing.
