Doumeng C, Maroux S
Biochem J. 1979 Mar 1;177(3):801-8. doi: 10.1042/bj1770801.
Aminotripeptidase, a cytosol enzyme from rabbit intestinal mucosa, was purified to homogeneity. The pure enzyme is a glycoprotein containing a very small amount of sugar. It is composed of only one subunit of 50,000 mol. wt. and possesses 1 zinc atom per molecule. Its specificity is primarily directed towards tripeptides with an N-terminal proline residue. However, the enzyme is also able to hydrolyse other tripeptides, except those with either a charged amino acid in the N-terminal position or a proline residue in the second position. The purified aminotripeptidase accounts for almost all the tripeptidase activity of the soluble fraction from intestinal mucosa.
氨基三肽酶是一种来自兔肠黏膜的胞质酶，已被纯化至同质。纯酶是一种含糖量极少的糖蛋白。它仅由一个分子量为50,000的亚基组成，每个分子含有1个锌原子。其特异性主要针对具有N端脯氨酸残基的三肽。然而，该酶也能够水解其他三肽，但N端位置带有带电氨基酸或第二位带有脯氨酸残基的三肽除外。纯化的氨基三肽酶几乎占肠黏膜可溶性部分所有三肽酶活性。
