| Literature DB >> 2869975 |
H R Scholte, I E Luyt-Houwen, M L Dubelaar, W C Hulsmann.
Abstract
The formation of malonyl-CoA in rat heart is catalyzed by cytosolic acetyl-CoA carboxylase. The existence of this enzyme in heart is difficult to prove by the abundant occurrence of mitochondrial propionyl-CoA carboxylase, which is also able to catalyze the carboxylation of acetyl-CoA. We used the calcium paradox as a tool to separate cytosolic components from the remaining heart, and found that acetyl-CoA carboxylase activity was preferentially released, like lactate dehydrogenase and carnitine, while propionyl-CoA carboxylase was almost fully retained. Acetyl-CoA carboxylase activity was determined after activation by citrate ion and Mg2+. The activity decreased to 64% by 48 h of fasting.Entities:
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Year: 1986 PMID: 2869975 DOI: 10.1016/0014-5793(86)81182-6
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124