肝脏α-淀粉酶的分离与研究。与糖原磷酸化酶活性的比较。
Isolation and study of a liver alpha-amylase. Comparison with glycogen phosphorylase activity.
作者信息
García-Valdés E, Busquets X, Cabello F M
出版信息
Rev Esp Fisiol. 1982 Jun;38(2):177-82.
PMID:6181541
Abstract
An oligomaltosaccharide-forming amylase has been observed in mice liver crude homogenate. This enzyme has been isolated by binding to amylose. Some of its functional parameters have been studied and compared with those of glycogen phosphorylase demonstrating that amylase activity is not due to a glycogen phosphorylase isoenzyme. It has been further observed that amylase needs Ca2+ of Mg+2 and Cl- for its activity.
摘要
在小鼠肝脏粗匀浆中观察到一种形成低聚麦芽糖的淀粉酶。该酶通过与直链淀粉结合而被分离出来。已经研究了它的一些功能参数，并与糖原磷酸化酶的参数进行了比较，结果表明淀粉酶活性并非源于糖原磷酸化酶同工酶。进一步观察到，淀粉酶的活性需要Ca2+、Mg+2和Cl-。
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