Hazato T, Shimamura M, Komuro T, Katayama T
Biochem Int. 1985 May;10(5):813-9.
In human cerebrospinal fluid, aminopeptidase, dipeptidyl aminopeptidase, dipeptidyl carboxypeptidase, and carboxypeptidase which were capable of hydrolyzing enkephalins were detected. Among these enzymes, two distinct aminopeptidase, designated C-AP1 and C-AP2, were partially purified. These enzymes were not purified thoroughly, but the characteristics of C-AP2 were similar to those of an aminopeptidase purified from monkey brain. But the inhibitory activity of amastatin on C-AP2 was stronger, and that of substance P was negligible. On the other hand, characteristics of C-Ap1 were extremely differ from those of C-AP2 or an aminopeptidase purified from monkey brain. C-AP1 had an optimum pH more in the acidic range (the highest at pH 6.0) and was not inhibited by any of the protease inhibitor tested including bestatin and amastatin.
在人类脑脊液中，检测到了能够水解脑啡肽的氨肽酶、二肽基氨肽酶、二肽基羧肽酶和羧肽酶。在这些酶中，两种不同的氨肽酶，分别命名为C-AP1和C-AP2，得到了部分纯化。这些酶没有被彻底纯化，但C-AP2的特性与从猴脑中纯化得到的一种氨肽酶相似。不过，抑氨肽素对C-AP2的抑制活性更强，而P物质的抑制活性可忽略不计。另一方面，C-Ap1的特性与C-AP2或从猴脑中纯化得到的氨肽酶截然不同。C-AP1在酸性范围内有一个最佳pH值（在pH 6.0时最高），并且不受包括抑氨肽酶和抑氨肽素在内的任何测试蛋白酶抑制剂的抑制。
