Ishiura S, Yamamoto T, Yamamoto M, Nojima M, Aoyagi T, Sugita H
National Institute of Neuroscience, NCNP, Tokyo.
J Biochem. 1987 Nov;102(5):1023-31. doi: 10.1093/oxfordjournals.jbchem.a122140.
Two major aminopeptidases, an aminopeptidase B and an aminopeptidase M-like enzyme, were purified from human skeletal muscle by DEAE-cellulose, HPLC gel filtration, and hydroxyapatite column chromatographies. The purified aminopeptidase B exhibits a molecular weight of 76,000 under both native and denaturing conditions. The activity of the aminopeptidase B is regulated by C1 ions and other anions in vitro. On the other hand, the aminopeptidase M-like enzyme is a monomeric protein having a molecular weight of 96,000. It is capable of significantly cleaving Phe-, Leu-, Arg-, and Ala-aminoacyl bonds in the presence of 2-mercaptoethanol. The pH optima for both enzymes are around 7.0, and bestatin is an effective inhibitor of both enzymes.
通过DEAE - 纤维素、高效液相色谱凝胶过滤和羟基磷灰石柱色谱法从人骨骼肌中纯化出两种主要的氨肽酶，一种氨肽酶B和一种类氨肽酶M。纯化后的氨肽酶B在天然和变性条件下的分子量均为76,000。氨肽酶B的活性在体外受氯离子和其他阴离子调节。另一方面，类氨肽酶M是一种分子量为96,000的单体蛋白。在2 - 巯基乙醇存在的情况下，它能够显著切割苯丙氨酸 - 、亮氨酸 - 、精氨酸 - 和丙氨酸 - 氨酰键。两种酶的最适pH值均约为7.0，抑肽素是这两种酶的有效抑制剂。
