磷酸化对钙蛋白酶II活性的调节——环amp依赖性蛋白激酶蛋白水解的变化(峰II, DEAE)。

Applied and theoretical electrophoresis : the official journal of the International Electrophoresis Society Pub Date : 1993-01-01

W N Kuo, U Ganesan, D L Walbey, D L Davis, K Allen, L K McCall

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引用次数: 0

摘要

采用sds -聚丙烯酰胺凝胶电泳和放射自显影技术分析32p标记的环amp依赖性蛋白激酶全酶(A-PKII:DEAE，峰II分数)的蛋白水解。A-PKII和calpain II的污染物显然不影响这种高灵敏度分析的准确性。环amp依赖性蛋白激酶(A-PK)的催化亚基对calpain II的磷酸化极大地促进了A-PKII的蛋白水解，而蛋白激酶C (PK-C)或环gmp依赖性蛋白激酶(G-PK)的磷酸化则略微改变了蛋白水解。

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Modulation of the activity of calpain II by phosphorylation--changes in the proteolysis of cyclic AMP-dependent protein kinase (peak II, DEAE).

The proteolysis of the 32P-labeled holoenzyme of cyclic AMP-dependent protein kinase (A-PKII:DEAE, peak II fraction) was analysed by SDS-polyacrylamide gel electrophoresis and autoradiography. The contaminants of the A-PKII and calpain II apparently did not interfere with the accuracy of this highly sensitive analysis. Phosphorylation of calpain II by the catalytic subunit of cyclic AMP-dependent protein kinase (A-PK) greatly enhanced the proteolysis of A-PKII, whereas phosphorylation by protein kinase C (PK-C) or cyclic GMP-dependent protein kinase (G-PK) slightly altered the proteolysis.

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Applied and theoretical electrophoresis : the official journal of the International Electrophoresis Society

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