兔小肠葡糖淀粉酶的动力学研究。
Kinetic studies on glucoamylase of rabbit small intestine.
作者信息
Sivakami S, Radhakrishnan A N
出版信息
Biochem J. 1976 Feb 1;153(2):321-7. doi: 10.1042/bj1530321.
Abstract
The kinetic properties of a maltase-glucoamylase complex with a neutral pH optimum, purified to homogeneity from the brush borders of the rabbit small intestine, are described. It has a broad range of substrate specificity, hydrolysing di- and poly-saccharides with alpha-1,4 and alpha-1,6 linkages. The Km and Vmax, values of the enzyme for the various substrates were determined. Starch and maltose were its best substrates. The kinetics of hydrolysis of two synthetic linear maltosaccharides, namely maltotriose and maltopentaose, were studied. Mixed-substrate incubation studies revealed the presence of at least two interacting sites on the enzyme, and the data were further analysed by the use of a number of non-substrate inhibitors.
摘要
本文描述了一种从兔小肠刷状缘纯化至同质的麦芽糖酶-葡糖淀粉酶复合物的动力学特性，其最适pH为中性。它具有广泛的底物特异性，能水解具有α-1,4和α-1,6糖苷键的二糖和多糖。测定了该酶对各种底物的米氏常数（Km）和最大反应速度（Vmax）值。淀粉和麦芽糖是其最佳底物。研究了两种合成线性麦芽寡糖（麦芽三糖和麦芽五糖）的水解动力学。混合底物孵育研究表明该酶上至少存在两个相互作用位点，并通过使用多种非底物抑制剂对数据进行了进一步分析。
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