[三肽H-苏氨酸-（O-叔丁基）-苯丙氨酸-脯氨酸-OH对大鼠小肠氨肽酶活性的抑制作用]
[Inhibition of aminopeptidase activity of rat small intestine by the tripeptide H-Thr-(O-tert. butyl)-Phe-Pro-OH].
作者信息
Friedrich M, Uhlig J, Noack R
出版信息
Acta Biol Med Ger. 1978;37(10):1513-22.
The hydrolysis of L-leucine-beta-naphthylamide and L-leucinamide by leucinaminopeptidase (E.C. 3.4.11.1) from bovine eye lens is inhibited by H-Thr (O-tert. butyl)-Phe-Pro-OH. The inhibitor constants are Ki = 1.5 . 10(-5) M and 0.8 . 10(-5) M, respectively. Both brush border peptidases, leucinarylamidase (E.C. 3.4.11.2) AND TRIPEPTIDASE (E.C. 3.4.11.4), are inhibited to a smaller extent (Ki = 0.8 . 10(-3) M). Mn++-ions activate the cytosolic leucinaminopeptidase but not the hydrolysis of leucinamide by the brush border arylamidase. The inhibition of the cytosolic leucinamidase by the peptide (Ki = 3.5 . 10(-4)) is twice as that of the brush border arylamidase.
来自牛眼晶状体的亮氨酰氨肽酶（E.C. 3.4.11.1）对L-亮氨酸-β-萘酰胺和L-亮氨酰胺的水解作用受到H-Thr（O-叔丁基）-Phe-Pro-OH的抑制。抑制剂常数分别为Ki = 1.5×10⁻⁵ M和0.8×10⁻⁵ M。两种刷状缘肽酶，亮氨酰胺酶（E.C. 3.4.11.2）和三肽酶（E.C. 3.4.11.4），受到的抑制程度较小（Ki = 0.8×10⁻³ M）。锰离子激活胞质亮氨酰氨肽酶，但不激活刷状缘芳基酰胺酶对亮氨酰胺的水解。该肽对胞质亮氨酰胺酶的抑制作用（Ki = 3.5×10⁻⁴）是刷状缘芳基酰胺酶的两倍。
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