Purification of skeletal muscle hexokinase by affinity elution chromatography.
Purification of skeletal muscle hexokinase by affinity elution chromatography.
复制标题
通过亲和洗脱色谱法纯化骨骼肌己糖激酶。
DOI：
10.1016/0003-2697(80)90461-3
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发表时间：
1980
影响因子：
2.9
通讯作者：
J. S. Easterby
中科院分区：
文献类型：
--
作者：
S. S. Qadri;J. S. Easterby
II 型己糖激酶 (EC 2.7.1.1) 已通过简单的程序从大鼠骨骼肌中纯化出来，包括 DEAE-纤维素色谱、磷酸纤维素亲和洗脱色谱以及 Sephadex G-200 凝胶过滤。制备均质酶的关键是亲和洗脱步骤，其中效应分子葡萄糖6-磷酸用作洗脱配体。通过该程序获得了 5300 倍的纯化，并且仅在亲和洗脱步骤中就获得了超过 400 倍的纯化。从 800 g 大鼠肢体中获得约 3.3 mg 均质己糖激酶，比活性为 120 单位/mg。
Type II hexokinase (EC 2.7.1.1) has been purified from rat skeletal muscle by a simple procedure involving chromatography on DEAE-cellulose, affinity elution chromatography from phosphocellulose, and gel filtration on Sephadex G-200. The key to the preparation of homogeneous enzyme is the affinity elution step in which an effector molecule, glucose 6-phosphate, is used as the eluting ligand. A 5300-fold purification is obtained by the procedure and over 400-fold purification is obtained in the affinity elution step alone. Approximately 3.3 mg of homogeneous hexokinase with a specific activity of 120 units/mg is obtained from 800 g of rat limb.