Alteration of acylphosphate formation of cardiac sarcoplasmic reticulum ATPase by calmodulin-dependent phosphorylation.

C Pifl, B Plank, G Hellmann, W Wyskovsky, J Suko
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引用次数: 1

Abstract

The calcium-dependent acylphosphate formed by the calcium transport ATPase of cardiac sarcoplasmic reticulum and the calcium-, calmodulin-dependent phosphoester(s) of sarcoplasmic reticulum fractions formed by a calcium-, calmodulin-dependent membrane-bound protein kinase can be distinguished by removal of calcium and/or magnesium by EDTA or hydroxylamine treatment of the acid denaturated membranes. Both procedures decompose the acylphosphate with little effect on the phosphoester(s). Calmodulin-dependent phosphorylation (2.44 nmol/mg SR protein) reduces the apparent K(Ca) of the acylphosphate steady state level of the calcium transport ATPase from 0.56 to 0.34 microM free calcium, without affecting the maximum phosphoenzyme level (0.93 versus 0.89 nmol/mg protein), and has little, if any, effect on the Hill-coefficient (1.32 versus 1.54).

钙调素依赖性磷酸化对心肌肌浆网atp酶酰基形成的影响。
由心肌肌浆网钙转运atp酶形成的钙依赖性酰基磷酸和由钙、钙调素依赖的膜结合蛋白激酶形成的肌浆网部分的钙、钙调素依赖的磷酸酯可以通过EDTA或羟胺处理酸变性膜去除钙和/或镁来区分。这两种方法都能分解酰基磷酸,对磷酸酯几乎没有影响。钙调素依赖性磷酸化(2.44 nmol/mg SR蛋白)降低了钙转运atp酶的酰基磷酸盐稳态水平的表观K(Ca),从0.56 μ m游离钙降至0.34 μ m游离钙,而不影响最大磷酸化酶水平(0.93对0.89 nmol/mg蛋白),并且对hill系数(1.32对1.54)几乎没有影响。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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