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Rabbit renal cortex was found to contain three types of glycogen synthase kinase (GSK). Cylic AMP-dependent protein kinase (GSK-C) accounted for only a small fraction of the total GSK activity. The predominant type of GSK (GSK-P) could be adsorbed to phosphocellulose, but not to DEAE cellulose. The other major type (GSK-D) could be adsorbed to DEAE cellulose and exhibited several peaks when eluted with a linear NaC1 gradient. GSK-P and GSK-D were not affected by cyclic AMP or by the heat-stable protein inhibitor of cyclic AMP-dependent protein kinase. This suggests that cyclic AMP-independent mechanisms may play a major role in regulation of GSK. Neither GSK-P nor GSK-D were associated with the major peak of histone, kinase, casein kinase, protamine kinase or phosvitin kinase. Therefore it cannot be assumed that these protein kinase activities can be used to monitor GSK activity.
E M Reimann, and
K K Schlender
May 1979,
FEBS letters,
E M Reimann, and
K K Schlender
October 1980,
Biochemical Society transactions,
E M Reimann, and
K K Schlender
October 1979,
The Journal of biological chemistry,
E M Reimann, and
K K Schlender
October 1982,
Archives of biochemistry and biophysics,
E M Reimann, and
K K Schlender
February 1982,
The Journal of biological chemistry,
E M Reimann, and
K K Schlender
January 1981,
The Journal of biological chemistry,
E M Reimann, and
K K Schlender
March 1982,
The Journal of biological chemistry,
E M Reimann, and
K K Schlender
May 1979,
The Journal of biological chemistry,
E M Reimann, and
K K Schlender
March 1981,
The Biochemical journal,
E M Reimann, and
K K Schlender
July 1981,
Experimental eye research,
