来自牛脑的能够水解寡聚脯氨酸的氨肽酶P。
Aminopeptidase P, capable of hydrolyzing oligoproline, from bovine brain.
作者信息
Maruyama S, Kobayashi T, Ohmori T, Tanaka H, Maeda H
机构信息
National Institute of Bioscience and Human-Technology, Agency of Industrial Science and Technology, Ibaraki, Japan.
出版信息
Biosci Biotechnol Biochem. 1994 Nov;58(11):2107-8. doi: 10.1271/bbb.58.2107.
An aminopeptidase P, capable of hydrolyzing oligoproline, was isolated from the homogenate of bovine brain. The molecular mass of the enzyme was 140 kDa by gel filtration. The enzyme was activated by Mn2+ and inhibited by o-phenanthroline. The enzyme hydrolyzed substrates such as Pro-Pro-Pro-Pro, Pro-Pro-Pro, and Pro-Pro to proline, and cleaved N-terminal amino acids from peptides containing penultimate prolines such as bradykinin and neuropeptide Y.
从牛脑匀浆中分离出一种能够水解寡聚脯氨酸的氨肽酶P。通过凝胶过滤法测得该酶的分子量为140 kDa。该酶被Mn2+激活，被邻菲罗啉抑制。该酶能将如Pro-Pro-Pro-Pro、Pro-Pro-Pro和Pro-Pro等底物水解为脯氨酸，并从含有倒数第二个脯氨酸的肽（如缓激肽和神经肽Y）中切割N端氨基酸。
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