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Effect of ionic strength on production of cAMP‐ and Ca 2+ ‐independent protein kinase from rat liver plasma membrane
Author(s) -
Hashimoto Eikichi,
Sakanoue Youichirou,
Mizuta Keiko,
Yamamura Hirohei
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80511-7
Subject(s) - protein kinase a , ionic strength , protease , cytosol , biochemistry , proteolysis , chemistry , membrane , kinase , phosphorylation , enzyme , microbiology and biotechnology , biology , aqueous solution
Production of cAMP‐ and Ca 2+ ‐independent protein kinase was stimulated when rat liver plasma membrane was incubated with increasing concentrations of NaCl. This protein kinase release was diminished by addition of protease inhibitor. The molecular mass of this enzyme was approx. 50 kDa and a high concentration of Mg 2+ was required for whole histone phosphorylation. These properties are similar to those of the protease‐activated form of protein kinase C. The NaCl effect could be replaced by other salts such as LiCl and NaHCO 3 . These results suggest that membrane‐bound protein kinase C is activated by limited proteolysis corresponding to an increase in ionic strength.