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从大鼠脑中纯化膜结合氨肽酶:氨肽酶M的鉴定。

Purification of membrane-bound aminopeptidase from rat brain: identification of aminopeptidase M.

作者信息

Gros C, Giros B, Schwartz J C

出版信息

Neuropeptides. 1985 Feb;5(4-6):485-8. doi: 10.1016/0143-4179(85)90060-5.

DOI:10.1016/0143-4179(85)90060-5
PMID:2860607
Abstract

Two different membrane-bound aminopeptidases were isolated from rat brain membranes, one with a puromycin sensitive activity and the other, not affected by 10 microM puromycin. The physicochemical, catalytic and immunological properties of the latter were compared to those of aminopeptidase M purified from rat kidney membranes and allowed us to conclude to large similarities between these two enzymes. Because the two brain aminopeptidases were both sensitive to bestatin, it remains to be established whether both or only aminopeptidase M is involved in endogenous enkephalin inactivation.

摘要

从大鼠脑膜中分离出两种不同的膜结合氨基肽酶,一种具有对嘌呤霉素敏感的活性,另一种不受10微摩尔嘌呤霉素的影响。将后者的物理化学、催化和免疫学特性与从大鼠肾膜中纯化的氨基肽酶M的特性进行比较,使我们得出这两种酶之间有很大相似性的结论。由于这两种脑氨基肽酶都对贝抑素敏感,因此仍有待确定内源性脑啡肽失活是由两者还是仅由氨基肽酶M参与。

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