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Yeast cyclic AMP‐dependent protein kinase
Author(s) -
Wingender-Drissen Ruth
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)81155-7
Subject(s) - protein kinase a , biochemistry , glycogen phosphorylase , phosphorylase kinase , yeast , protein subunit , saccharomyces cerevisiae , glycogen synthase , enzyme , chemistry , biology , microbiology and biotechnology , gene
We have purified cyclic AMP‐dependent protein kinase from the yeast Saccharomyces cerevisiae . The purified enzyme was inactive in the absence of cyclic AMP and displayed two protein bands on SDS gel electrophoresis. One was identified as the cAMP‐binding protein by chromatography on cAMP‐agarose. M r of the latter was 50 000 while the catalytic subunit had an M r of 59 000. The enzyme accepted yeast phosphorylase, glycogen synthase and fructose 1,6‐bisphosphatase as substrates. No inhibition by the mammalian protein kinase inhibitor was observed.