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A newly discovered cyclic AMP-independent protein kinase, which catalyzes the total conversion of glycogen synthase from the I- to the D-form, has been isolated from rabbit skeletal muscle. This enzyme, designated glycogen synthase kinase, is separable from cyclic AMP-dependent protein kinase by column chromatography on phosphocellulose. Synthase kinase and cyclic AMP-dependent protein kinase are distinct in their specificity for protein substrates, the effects of cyclic AMP and the inhibitor of cyclic AMP-dependent protein kinase on their activities, and the extent to which they phosphorylate I-form glycogen synthase. The phosphorylation of I-form enzyme by synthase kinase results in the incorporation of 4 mol of phosphate/85,000 subunit; however only two of the phosphate sites seem predominantly to determine glucose-6-P dependence. The resulting multiply phosphorylated enzyme, which is highly dependent on glucose-6 P for activity, has a phosphate content comparable to the D-form enzyme isolated from rabbit muscle.
E Itarte, and
J C Robinson, and
K P Huang
October 1979,
The Journal of biological chemistry,
E Itarte, and
J C Robinson, and
K P Huang
March 1982,
The Journal of biological chemistry,
E Itarte, and
J C Robinson, and
K P Huang
January 1978,
Biochemical Society transactions,
E Itarte, and
J C Robinson, and
K P Huang
January 1981,
The Journal of biological chemistry,
E Itarte, and
J C Robinson, and
K P Huang
May 1979,
The Journal of biological chemistry,
E Itarte, and
J C Robinson, and
K P Huang
June 1980,
European journal of biochemistry,
E Itarte, and
J C Robinson, and
K P Huang
October 1980,
Biochimica et biophysica acta,
E Itarte, and
J C Robinson, and
K P Huang
April 1980,
The Journal of biological chemistry,
E Itarte, and
J C Robinson, and
K P Huang
January 1975,
Biochemistry,
E Itarte, and
J C Robinson, and
K P Huang
January 1981,
FEBS letters,
