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Phosphoenolpyruvate‐dependent protein kinase activity in rat skeletal muscle
Author(s) -
Khandelwal Ramji L.,
Mattoo Roshan L.,
Bruce Waygood E.
Publication year - 1983
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(83)81063-1
Subject(s) - skeletal muscle , phosphoenolpyruvate carboxykinase , chemistry , protein kinase a , microbiology and biotechnology , kinase , biochemistry , biology , endocrinology , enzyme
Phosphoenolpyruvate‐dependent protein kinase activity has been demonstrated in the soluble fraction of rat skeletal muscle. The reaction was not due to the formation of ATP in the incubation mixture. Cyclic AMP, calcium, ATP and a number of phosphate acceptor proteins did not stimulate the reaction. One 32 P‐labelled protein ( M r 25 000) was observed on SDS gels. The phosphorylated protein contained acid stable phosphoserine as a major phosphorylated amino acid. The phosphorylation reaction in crude extracts was not directly proportional to the amount of protein, but typical of a two‐component system; i.e., kinase and substrate. The chromatography of soluble proteins on Ultrogel AcA44 separated the phosphate acceptor protein(s) from the phosphoenolpyruvate‐dependent protein kinase activity.