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A new heparin‐inhibited and polyamine‐activated protein kinase from bovine kidney
Author(s) -
Singh Toolsee J.
Publication year - 1989
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(89)80147-4
Subject(s) - polyamine , heparin , chemistry , protein kinase a , biochemistry , microbiology and biotechnology , kinase , pharmacology , biology
Two casein kinases, casein kinase‐1 (CK‐1) and casein kinase‐2 (CK‐2), have been characterized from many sources. In this study we describe the properties of a third casein kinase, designated casein kinase‐3 (CK‐3). CK‐3 ( M r 32 000) is readily separated from CK‐2 by gel filtration and from CK‐1 by hydroxyapatite chromatography. CK‐3 phosphorylates several proteins, including phosphorylase kinase. Phosphorylation of phosphorylase kinase by CK‐3 results in a 10‐fold enzyme activation. CK‐3 is activated by spermine and inhibited by heparin, ADP, and divalent metal ions (Mn 2+ , Zn 2+ ). Heparin inhibition of the kinase is reversed by spermine. The physical and regulatory properties of CK‐3 are very similar to CK‐1, suggesting that these kinases may be closely related.