PMID: 6111734Dec 1, 1980Paper

Heat activation of rat epididymal fat tissue acetyl-coa carboxylase is due to dephosphorylation by its endogenous phosphatase

Lipids
G R Krakower, K H Kim

Abstract

Acetyl-CoA carboxylase from rat epididymal fat tissue is activated by incubation at 30 C in the absence of citrate or metal ions. This activation is accompanied by a corresponding loss of 32P from the labeled enzyme, and it is not blocked by the heat-stable phosphorylase phosphatase inhibitor proteins from rabbit muscle. We have succeeded in separating an activity which activates and dephosphorylates acetyl-CoA carboxylase from the carboxylase using polyethylene glycol-6000. These results suggest that the temperature-dependent activation of acetyl-CoA carboxylase in crude or partially purified preparations results from dephosphorylation of the carboxylase by bound phosphatase.

References

Oct 1, 1974·Archives of Biochemistry and Biophysics·C A Carlson, K H Kim
Oct 1, 1974·Archives of Biochemistry and Biophysics·C A Carlson, K H Kim
Jan 29, 1980·Biochemical and Biophysical Research Communications·G R Krakower, K H Kim

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Citations

Oct 1, 1982·Archives of Biochemistry and Biophysics·B A Clarke, S D Clarke
Jan 1, 1985·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·M N Abdel-Halim, S I Farah
Sep 1, 1983·European Journal of Biochemistry·K Wada, T Tanabe
Oct 31, 1983·Biochemical and Biophysical Research Communications·S D Clarke
Jul 31, 1985·Biochemical and Biophysical Research Communications·G R Krakower, K H Kim

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