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The major endogenous bovine brain protein kinase C inhibitor is a heat‐labile protein
Author(s) -
Fraser Elaine D.,
Walsh Michael P.
Publication year - 1991
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(91)81450-m
Subject(s) - protein kinase a , cytosol , biochemistry , phosphatase , endogeny , mitogen activated protein kinase kinase , chemistry , cgmp dependent protein kinase , protease , inhibitor protein , enzyme , protein kinase c , kinase , biology , microbiology and biotechnology
A crude cytosolic fraction prepared from bovine brain contained protein kinase C, as shown by immunoblotting, but its activity was undetectable, suggesting the presence of interfering factors. Phosphatase, ATPase and protease activities did not account for the absence of detectable protein kinase C activity. The major contributing factor was found to be a heat‐labile protein which was separated from the kinase by ion‐exchange chromatography. The contribution to the total inhibitory activity of heat‐stable proteins was relatively minor, suggesting that they may not function physiologically as protein kinase C inhibitors.