ENKEPHALIN CONVERTASE - PURIFICATION AND CHARACTERIZATION OF A SPECIFIC ENKEPHALIN-SYNTHESIZING CARBOXYPEPTIDASE LOCALIZED TO ADRENAL CHROMAFFIN GRANULES
ENKEPHALIN CONVERTASE - PURIFICATION AND CHARACTERIZATION OF A SPECIFIC ENKEPHALIN-SYNTHESIZING CARBOXYPEPTIDASE LOCALIZED TO ADRENAL CHROMAFFIN GRANULES
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DOI：
10.1073/pnas.79.12.3886
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发表时间：
1982-01-01
期刊：
影响因子：
--
通讯作者：
SNYDER, SH
中科院分区：
文献类型：
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作者：
FRICKER, LD;SNYDER, SH
一种特殊的羧肽酶转化脑啡肽前体脑啡肽在[牛]肾上腺嗜铬颗粒进行了纯化和鉴定。在肾上腺中，这种酶被称为脑啡肽转化酶，仅定位于嗜铬颗粒，其中含有脑啡肽和前体肽。与溶酶体羧肽酶不同，脑啡肽转化酶被氯化钴显著刺激，并被EDTA或1，10-菲咯啉抑制。纯化的酶对六肽[Met 5]-和[Leu 5]脑啡肽-Arg 6具有高亲和力（分别为51和83 μ M），对六肽[Met 5]-和[Leu 5]脑啡肽-Lys 6具有稍低的亲和力（195和174 μ M）。脑啡肽转化酶显示10倍的区域变化，不像其他羧肽酶，这是均匀分布。脑啡肽转化酶似乎与脑啡肽的生物合成选择性和生理性相关。
A specific carboxypeptidase that converts enkephalin precursors into enkephalin in [bovine] adrenal chromaffin granules was purified and characterized. In the adrenal this enzyme, designated enkephalin covertase, 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 .mu.M, respectively) and a somewhat lower affinity for the hexapeptides [Met5]- and [Leu5]enkephalin-Lys6 (195 and 174 .mu.M). 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.