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• W2023344829 abstract "Investigation of the intracellular localization of the principal enzymes involved in the formation and breakdown of β-hydroxy-β-methyl-glutaryl CoA (HMG CoA) in rat liver has shown that HMG CoA condensing and cleavage enzymes are both preponderantly in the mitochondria. HMG CoA reductase, which leads to the pathway of cholesterol synthesis, is in the microsomes, and is only one twentieth as active as the cleavage enzyme which leads to acetoacetate production. In spite of this unfavorable ratio, cholesterol synthesis does occur—possibly because a small amount of condensing enzyme and most or all of the reductase are in the microsomes which are low in cleavage activity. Stimulation of cholesterol synthesis by injection of Triton, or inhibition by fasting does not importantly alter the amount or distribution of the condensing and cleavage enzymes. However, a severe depression of reductase activity in fasting suggests that this may be a significant factor in the rate limitation of cholesterol synthesis in this condition." @default.
• W2023344829 created "2016-06-24" @default.
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• W2023344829 date "1960-01-01" @default.
• W2023344829 modified "2023-09-25" @default.
• W2023344829 title "β-hydroxy-β-methylglutaryl coenzyme a reductase, cleavage and condensing enzymes in relation to cholesterol formation in rat liver" @default.
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• W2023344829 doi "https://doi.org/10.1016/0006-3002(60)91390-1" @default.
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