纯化的牛心和大鼠肝脏6-磷酸果糖-2-激酶的比较。不同同工酶的证据。
Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Evidence for distinct isoenzymes.
作者信息
Rider M H, Foret D, Hue L
出版信息
Biochem J. 1985 Oct 1;231(1):193-6. doi: 10.1042/bj2310193.
Abstract
Rat liver and bovine heart 6-phosphofructo-2-kinase were purified by the same procedure. Compared with the liver enzyme, the heart enzyme had a smaller apparent Mr, different kinetic properties, was not inactivated by cyclic AMP-dependent protein kinase, and contained less fructose-2,6-bisphosphatase activity. These differences suggest that heart and liver 6-phosphofructo-2-kinase are distinct isoenzymes. Likewise, 6-phosphofructo-2-kinase from rat heart and skeletal muscle was not inactivated on treatment with cyclic AMP-dependent protein kinase.
摘要
大鼠肝脏和牛心脏的6-磷酸果糖-2-激酶通过相同的程序进行纯化。与肝脏酶相比，心脏酶的表观分子量较小，具有不同的动力学特性，不会被环磷酸腺苷依赖性蛋白激酶灭活，并且果糖-2,6-双磷酸酶活性较低。这些差异表明心脏和肝脏的6-磷酸果糖-2-激酶是不同的同工酶。同样，大鼠心脏和骨骼肌的6-磷酸果糖-2-激酶在用环磷酸腺苷依赖性蛋白激酶处理后不会被灭活。
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