脑啡肽转换酶：一种定位于肾上腺嗜铬颗粒的特异性脑啡肽合成羧肽酶的纯化及特性研究
Enkephalin convertase: purification and characterization of a specific enkephalin-synthesizing carboxypeptidase localized to adrenal chromaffin granules.
作者信息
Fricker L D, Snyder S H
出版信息
Proc Natl Acad Sci U S A. 1982 Jun;79(12):3886-90. doi: 10.1073/pnas.79.12.3886.
Abstract
A specific carboxypeptidase that converts enkephalin precursors into enkephalin in adrenal chromaffin granules has been purified and characterized. In the adrenal this enzyme, designated enkephalin convertase, is uniquely localized to the chromaffin granules, which contain enkephalin and precursor peptides. Enkephalin convertase is markedly stimulated by CoCl2 and inhibited by EDTA or 1,10-phenanthroline, unlike the lysosomal carboxypeptidase. The purified enzyme has a high affinity for the hexapeptides [Met5]- and [Leu5]enkephalin-Arg6 (51 and 83 microM, respectively) and a somewhat lower affinity for the hexapeptides [Met5]- and [Leu5]enkephalin-Lys6 (195 and 174 microM). Brain enkephalin convertase shows 10-fold regional variations, unlike other carboxypeptidases, which are uniformly distributed. Enkephalin convertase appears to be associated selectively and physiologically with biosynthesis of the enkephalins.
摘要
一种能将脑啡肽前体转化为肾上腺嗜铬颗粒中的脑啡肽的特异性羧肽酶已被纯化并鉴定。在肾上腺中，这种被称为脑啡肽转化酶的酶独特地定位于含有脑啡肽和前体肽的嗜铬颗粒中。与溶酶体羧肽酶不同，脑啡肽转化酶受到CoCl2的显著刺激，并被EDTA或1,10 - 菲咯啉抑制。纯化后的酶对六肽[Met5]-和[Leu5]脑啡肽 - Arg6（分别为51和83 microM）具有高亲和力，对六肽[Met5]-和[Leu5]脑啡肽 - Lys6（195和174 microM）的亲和力略低。与其他均匀分布的羧肽酶不同，脑啡肽转化酶在脑中呈现出10倍的区域差异。脑啡肽转化酶似乎在生理上与脑啡肽的生物合成选择性相关。
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