大鼠肝脏腺苷5'-三磷酸-D-葡萄糖6-磷酸转移酶的纯化及性质
Purification and properties of adenosine 5'-triphospae-D-glucose 6-phosphotransferase from rat liver.
作者信息
Parry M J, Walker D G
出版信息
Biochem J. 1966 May;99(2):266-74. doi: 10.1042/bj0990266.
Abstract
- An 870-fold purification of glucokinase from rat liver is described which involves ammonium sulphate fractionation and the use of DEAE-Sephadex, DEAE-cellulose and polyacrylamide columns. 2. The preparation is free of any interfering enzymes and has a specific activity of 8mumoles/min./mg. of protein. 3. Glucokinase catalyses the phosphorylation of glucose, mannose and 2-deoxyglucose. 4. The enzyme is inhibited by high concentrations of glucose 6-phosphate only; ADP is an inhibitor whose effect depends on the Mg(2+) concentration. 5. The properties of glucokinase are compared briefly with those of other phosphotransferases.
摘要
- 本文描述了从大鼠肝脏中纯化葡萄糖激酶的方法，该方法经过870倍纯化，包括硫酸铵分级分离以及使用二乙氨基乙基葡聚糖（DEAE - Sephadex）、二乙氨基乙基纤维素（DEAE - cellulose）和聚丙烯酰胺柱。2. 该制剂不含任何干扰酶，比活性为8微摩尔/分钟/毫克蛋白质。3. 葡萄糖激酶催化葡萄糖、甘露糖和2 - 脱氧葡萄糖的磷酸化。4. 该酶仅受高浓度葡萄糖6 - 磷酸的抑制；二磷酸腺苷（ADP）是一种抑制剂，其作用取决于镁离子（Mg(2+)）浓度。5. 将葡萄糖激酶的特性与其他磷酸转移酶的特性进行了简要比较。
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