HEAT ACTIVATION OF RAT-LIVER ACETYL-COA CARBOXYLASE INVITRO
- 1 January 1978
- journal article
- letter
- Vol. 253 (14) , 4826-4829
Abstract
Acethyl-CoA carboxylase [EC 6.4.1.2] in rat liver homogenates was activated in vitro in a time- and temperature-dependent manner. The activity of acetyl-CoA carboxylase in rat liver preparations was determined in a 1 min assay to preclude the possibility of citrate activation of the enzyme during the assay period. Activation of the enzyme during the assay period. Activation of the enzyme occurred more rapidly in liver preparations continuously maintained at ambient or greater temperatures than in homogenates of liver which had been chilled. High speed supernatant (105,000 .times. g, 60 min) did not heat-activate, and reconstitution of the heat-activatable 27,000 .times. g, 20 min, fraction by recombining the high speed pellet with the high speed supernatant only partially restored the heat activatability. Elution of the 105,000 .times. g supernatant from Sephadex G-25 resulted in an enzyme preparation which was heat-activatable. Addition of boiled 105,000 .times. g supernatant to the Sephadex G-25-treated enzyme again prevented heat activation. Dilution of the enzyme 5-fold did not prevent heat activation.This publication has 4 references indexed in Scilit:
- Regulation of rat liver acetyl coenzyme A carboxylase. Evidence for interconversion between active and inactive forms of enzyme by phosphorylation and dephosphorylation.Journal of Biological Chemistry, 1977
- Activation of soluble guanylate cyclase from rat lung by incubation or by hydrogen peroxide.Journal of Biological Chemistry, 1976
- Time-dependent increase in rat liver glycogen synthetase activity in vitroArchives of Biochemistry and Biophysics, 1967
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