[猪胰腺α-淀粉酶在去除结构钙后的蛋白水解敏感性]

[Proteolytic susceptibility of alpha-amylase of the pancreas of swine deprived of its structural calcium].

作者信息

Milicua J C, García F A, Macarulla J M

出版信息

Rev Esp Fisiol. 1986 Sep;42(3):355-8.

Abstract

Hog pancreas alpha-amylase (alpha-1-4-glucan-glucan hydrolase, E.C. 3.2.1.1) lost its structural calcium by action of EDTA at 20 degrees C. Enzymatic activity experimented a decrease whereas a big increase in proteolytic susceptibility to bovine pancreas trypsin (E.C. 3.4.4.4) was shown. Native alpha-amylase had an activity of 2,730 mg maltose/min X mg enzyme and a Km of 0.222% amylose, the activity of calcium depleted amylase being of 1,640 mg maltose/min X mg enzyme and Km 0.571% amylose. Simple methods for evaluating proteolytic susceptibility of alpha-amylase micro-amounts against trypsin action, and for the measurement of alpha-amylase activity in polyacrylamide rod gels were also described.

摘要

猪胰α-淀粉酶（α-1-4-葡聚糖-葡聚糖水解酶，E.C. 3.2.1.1）在20℃下经EDTA作用失去其结构钙。酶活性降低，而对牛胰蛋白酶（E.C. 3.4.4.4）的蛋白水解敏感性则大幅增加。天然α-淀粉酶的活性为2730毫克麦芽糖/分钟×毫克酶，米氏常数为0.222%直链淀粉，脱钙淀粉酶的活性为1640毫克麦芽糖/分钟×毫克酶，米氏常数为0.571%直链淀粉。还描述了评估微量α-淀粉酶对胰蛋白酶作用的蛋白水解敏感性以及在聚丙烯酰胺棒状凝胶中测量α-淀粉酶活性的简单方法。