Ulrich C, Hersh L B
Peptides. 1985 May-Jun;6(3):475-82. doi: 10.1016/0196-9781(85)90113-5.
Fractionation of Triton-solubilized rat brain membranes on diethylaminoethyl-cellulose resolves two peptidases which hydrolyze beta-neo-endorphin. One of these peptidases was identified as Angiotensin Converting Enzyme by (a) its sensitivity to inhibition by the specific inhibitors MK422 and captopril, (b) by the identification of reaction products, and (c) by comparison to authentic angiotensin converting enzyme. In contrast, alpha-neo-endorphin hydrolysis by angiotensin converting enzyme could not be detected. The second enzyme active on beta-neo-endorphin was identified as an aminopeptidase. This aminopeptidase is identical to the previously described enkephalin-degrading aminopeptidase. The possible involvement of these enzymes in the metabolism of opioid peptides is discussed.
用二乙氨基乙基纤维素对经曲拉通溶解的大鼠脑膜进行分级分离，可分离出两种能水解β-新内啡肽的肽酶。其中一种肽酶被鉴定为血管紧张素转换酶，依据如下：（a）其对特异性抑制剂MK422和卡托普利抑制作用的敏感性；（b）反应产物的鉴定；（c）与 authentic血管紧张素转换酶的比较。相比之下，未检测到血管紧张素转换酶对α-新内啡肽的水解作用。另一种作用于β-新内啡肽的酶被鉴定为氨肽酶。这种氨肽酶与先前描述的脑啡肽降解氨肽酶相同。文中讨论了这些酶在阿片肽代谢中可能的作用。
