Sullivan S, Akil H, Blacker D, Barchas J D
Peptides. 1980 Spring;1(1):31-5. doi: 10.1016/0196-9781(80)90032-7.
There are at least two types of enzymes in brain, endopeptidases and aminopeptidases, which metabolize enkephalins. Evidence is presented to suggest that enkephalinase, an endopeptidase cleaving at the Gly-Phe bond, is specific for the endogenous enkephalinergic system. Selective inhibitors are described for each enzyme. These are parachloromercuriphenylsulfonic acid and puromycin in the case of aminopeptidases and various enkephalin fragments in the case of enkephalinase. Some characteristics of the two types of enzymes are described. Enkephalinase has many properties in common with the well-characterized brain angiotensin-converting enzyme. These two enzymes, however, behaved differently when tested for chloride dependence, for activity in several buffers and for susceptibility to specific inhibitors.
大脑中至少存在两种酶，即内肽酶和氨肽酶，它们可代谢脑啡肽。有证据表明，脑啡肽酶作为一种在内啡肽甘氨酸 - 苯丙氨酸键处裂解的内肽酶，对体内源性脑啡肽能系统具有特异性。文中描述了针对每种酶的选择性抑制剂。对于氨肽酶而言，这些抑制剂是对氯汞苯磺酸和嘌呤霉素；对于脑啡肽酶而言，则是各种脑啡肽片段。文中还描述了这两种酶的一些特性。脑啡肽酶与已被充分研究的脑内血管紧张素转换酶有许多共同特性。然而，在测试对氯化物的依赖性、在几种缓冲液中的活性以及对特定抑制剂的敏感性时，这两种酶的表现有所不同。
