来自兔肾皮质的中性麦芽糖酶/葡糖淀粉酶。
Neutral maltase/glucoamylase from rabbit renal cortex.
作者信息
Pereira B, Sivakami S
机构信息
Department of Life Sciences, University of Bombay, India.
出版信息
Biochem J. 1989 Jul 1;261(1):43-7. doi: 10.1042/bj2610043.
Abstract
Maltase activity (EC 3.2.1.20) was solubilized from rabbit kidney brush-border membrane by using 1.0% Triton X-100 and purified 230-fold with an overall recovery of 30%. The purification procedure makes use of heat precipitation, chromatography on DE-52 DEAE-cellulose and gel filtration on Sephacryl S-300. Rabbit kidney brush border exhibited glucoamylase activity with a maltase/glucoamylase ratio of 1.5:1 to 2.0:1. During purification the maltase and glucoamylase activities behaved identically. The Mr of the complex is 590,000, and it appears to be composed of eight identical subunits linked by disulphide bridges.
摘要
通过使用1.0%的 Triton X-100从兔肾刷状缘膜中溶解麦芽糖酶活性（EC 3.2.1.20），并进行了230倍的纯化，总回收率为30%。纯化过程利用了热沉淀、DE-52 DEAE-纤维素柱色谱和Sephacryl S-300凝胶过滤。兔肾刷状缘表现出葡糖淀粉酶活性，麦芽糖酶/葡糖淀粉酶的比例为1.5:1至2.0:1。在纯化过程中，麦芽糖酶和葡糖淀粉酶的活性表现相同。该复合物的分子量为590,000，似乎由通过二硫键连接的八个相同亚基组成。
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引用本文的文献
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A comparison of the active site of maltase-glucoamylase from the brush border of rabbit small intestine and kidney by chemical modification studies.
Biochem J. 1991 Mar 1;274 ( Pt 2)(Pt 2):349-54. doi: 10.1042/bj2740349.
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