Szücs K, Vereb G, Bot G
Int J Biochem. 1983;15(9):1161-7. doi: 10.1016/0020-711x(83)90232-x.
Pseudo first order rate constants were determined for the dephosphorylation of heart and skeletal muscle specific phosphorylase a isoenzymes isolated from rabbit and pig using rabbit muscle phosphorylase phosphatase (mol. wt 34,000). The rate constants determined in the absence of ligands, were 4-5 fold lower for heart specific phosphorylases than for skeletal muscle specific ones. Glucose 6-phosphate (0.5-1 mM) enhances the rate of dephosphorylation of heart specific isophosphorylases 3-fold and suspends inhibition by 10(-5) M AMP, however, it has no significant effect on the dephosphorylation of skeletal muscle specific enzymes under the same conditions. Our data support characteristic functional differences between heart and skeletal muscle specific phosphorylases both in rabbit and pig.
使用兔肌肉磷酸化酶磷酸酶(分子量34,000)测定了从兔和猪分离的心脏和骨骼肌特异性磷酸化酶a同工酶去磷酸化的伪一级速率常数。在无配体情况下测定的速率常数,心脏特异性磷酸化酶比骨骼肌特异性磷酸化酶低4至5倍。6-磷酸葡萄糖(0.5 - 1 mM)可使心脏特异性异磷酸化酶的去磷酸化速率提高3倍,并消除10(-5) M AMP的抑制作用,然而,在相同条件下,它对骨骼肌特异性酶的去磷酸化没有显著影响。我们的数据支持兔和猪心脏与骨骼肌特异性磷酸化酶之间存在特征性功能差异。