Avakian E A, Ritov V B, Kozlov Iu P
Biokhimiia. 1980 Apr;45(4):601-8.
The effect of cAMP-dependent protein kinases from rabbit skeletal muscles on Ca2+ uptake by fragments of skeletal muscle sarcoplasmic reticulum was studied. It was shown that incubation of the sarcoplasmic reticulum fragments with protein kinase increases the rate of Ca2+ uptake without changing the activity of Ca2+-dependent ATPase. This phenomenon is not accompanied by phosphorus incorporation into the protein components of the reticulum membranes. The protein kinase preparation subjected to "self-phosphorylation" is also capable to increase the rate of Ca2+ uptake. Using (14C) -oleic acid, it was shown that the increase of the rate of Ca2+ transport under effects of the "self-phosphorylated" protein kinase occurs due to the binding of free fatty acids present in the sarcoplasmic reticulum membranes. It was found that the effect observed is due to phosphofructokinase (ATP : D-fructose-6-phosphate-1-phosphotransferase) present in the protein kinase preparation.
研究了来自兔骨骼肌的环磷酸腺苷(cAMP)依赖性蛋白激酶对骨骼肌肌浆网片段摄取钙离子的影响。结果表明,将肌浆网片段与蛋白激酶一起孵育可提高钙离子摄取速率,而不改变钙离子依赖性ATP酶的活性。这种现象并不伴随着磷掺入网状膜的蛋白质成分中。经过“自身磷酸化”的蛋白激酶制剂也能够提高钙离子摄取速率。使用(14C)-油酸表明,在“自身磷酸化”蛋白激酶的作用下,钙离子转运速率的提高是由于肌浆网膜中存在的游离脂肪酸的结合。研究发现,观察到的这种作用是由于蛋白激酶制剂中存在的磷酸果糖激酶(ATP:D-果糖-6-磷酸-1-磷酸转移酶)所致。