来自普通小麦的II型α-淀粉酶抑制剂对人唾液α-淀粉酶的抑制作用具有竞争性、缓慢且紧密结合的特点。

The inhibition of human salivary alpha-amylase by type II alpha-amylase inhibitor from Triticum aestivum is competitive, slow and tight-binding.

作者信息

Goff D J, Kull F J

机构信息

Department of Chemistry, Dartmouth College Hanover, New Hampshire 03755, USA.

出版信息

J Enzyme Inhib. 1995;9(2):163-70. doi: 10.3109/14756369509042815.

DOI:10.3109/14756369509042815

PMID:8583253

Abstract

A kinetic analysis of the inhibition of human salivary alpha-amylase (EC 3.2.1.1) by wheat seed (Triticum aestivum) type II alpha-amylase inhibitor revealed the inhibition was slow and tight-binding. The inhibition was competitive with an inhibition binding constant of the alpha-amylase inhibitor for alpha-amylase of 0.29 nM. The KM of alpha-amylase for soluble starch (calculated per mole of alpha-1,4 linked maltose residues) was 5.87 mM.

摘要

对小麦种子（普通小麦）II型α-淀粉酶抑制剂抑制人唾液α-淀粉酶（EC 3.2.1.1）的动力学分析表明，这种抑制作用缓慢且具有紧密结合性。该抑制作用具有竞争性，α-淀粉酶抑制剂对α-淀粉酶的抑制结合常数为0.29 nM。α-淀粉酶作用于可溶性淀粉的米氏常数（按每摩尔α-1,4连接的麦芽糖残基计算）为5.87 mM。