Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Evidence for distinct isoenzymes.
Comparison of purified bovine heart and rat liver 6-phosphofructo-2-kinase. Evidence for distinct isoenzymes.
复制标题
纯化牛心脏和大鼠肝脏 6-磷酸果糖-2-激酶的比较。
作者：
M. Rider;D. Foret;L. Hue
大鼠肝脏和牛心脏6-磷酸果糖-2-激酶的纯化通过相同的程序。与肝酶相比，心脏酶具有较小的表观Mr，不同的动力学性质，不被环AMP依赖性蛋白激酶灭活，并且含有较少的果糖-2，6-二磷酸酶活性。这些差异表明，心脏和肝脏6-磷酸果糖-2-激酶是不同的同工酶。同样，6-磷酸果糖-2-激酶从大鼠心脏和骨骼肌不灭活治疗与环AMP依赖性蛋白激酶。
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.