Szechinski J, Hsia W C, Behal F J
Enzyme. 1983;29(1):21-31. doi: 10.1159/000469600.
Two closely related but different aminopeptidases from bovine lung have been isolated and characterized. The first aminopeptidase, which removes the N-terminal arginine residue from L-arginyl-L-prolyl-L-proline, bradykinin, and des-[Arg9]-bradykinin, has kininase activity; it has a pH optimum of 8.0, is stimulated by Mn2+, and its molecular weight in dilute buffers is slightly greater than 240,000 daltons. The second aminopeptidase, which converts kallidin to bradykinin, has kinin-converting activity; it has a pH optimum of 6.8, is stimulated by Co2+, and its molecular weight in dilute buffers is 250,000 daltons. The kinin-converting enzyme is blocked from action when the N-terminal penultimate residue is proline.
已从牛肺中分离并鉴定出两种密切相关但不同的氨肽酶。第一种氨肽酶可从L-精氨酰-L-脯氨酰-L-脯氨酸、缓激肽和去[Arg9]-缓激肽中去除N端精氨酸残基，具有激肽酶活性；其最适pH为8.0，受Mn2+刺激，在稀缓冲液中的分子量略大于240,000道尔顿。第二种氨肽酶可将胰激肽转化为缓激肽，具有激肽转化活性；其最适pH为6.8，受Co2+刺激，在稀缓冲液中的分子量为250,000道尔顿。当倒数第二个N端残基为脯氨酸时，激肽转化酶的作用被阻断。
