α-葡萄糖苷酶抑制剂对人胰腺和唾液α-淀粉酶的作用。

Effect of alpha-glucosidase inhibitor on human pancreatic and salivary alpha-amylase.

作者信息

Suehiro I, Otsuki M, Yamasaki T, Ohki A, Sakamoto C, Yuu H, Maeda M, Baba S

出版信息

Clin Chim Acta. 1981 Dec 9;117(2):145-52. doi: 10.1016/0009-8981(81)90035-8.

Abstract

The mode of inhibition of a new complex oligosaccharide that inhibits the alpha-glucoside hydrolase activity of pancreatic and salivary alpha-amylase was studied. Kinetic analysis revealed a non-competitive type of inhibition with a Ki of 1.47 +/- 0.03 micrograms when tested against human pancreatic alpha-amylase and 3.89 +/- 0.08 micrograms against human salivary alpha-amylase. The inhibitory action of alpha-glucoside hydrolase inhibitor (alpha-GHI) on pancreatic amylase was observed over a wide range of pH (6.0--7.9), whereas the inhibition of salivary amylase was optimal at pH 6.5. Column chromatographic investigations suggested the possible formation of an enzyme-inhibitor complex because the mixture of alpha-GHI and pancreatic alpha-amylase was eluted as a single component through a Sephadex G200 column. However, this enzyme-inhibitor complex was easily separated into each component and the enzyme activity was fully recovered after electrophoresis.

摘要

研究了一种新型复合寡糖对胰腺和唾液α-淀粉酶的α-葡萄糖苷水解酶活性的抑制方式。动力学分析显示，在针对人胰腺α-淀粉酶进行测试时，该抑制作用为非竞争性类型，抑制常数（Ki）为1.47±0.03微克；针对人唾液α-淀粉酶时，Ki为3.89±0.08微克。α-葡萄糖苷水解酶抑制剂（α-GHI）对胰腺淀粉酶的抑制作用在较宽的pH范围（6.0 - 7.9）内均可观察到，而对唾液淀粉酶的抑制作用在pH 6.5时最为显著。柱色谱研究表明可能形成了酶-抑制剂复合物，因为α-GHI与胰腺α-淀粉酶的混合物通过Sephadex G200柱作为单一成分被洗脱。然而，这种酶-抑制剂复合物很容易分离成各组分，并且在电泳后酶活性完全恢复。