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- W1966929750 abstract "The role of ATP citrate lyase (ATP: citrate oxaloacetate-lyase (CoA-acetylating and ATP-dephosphorylating), EC 4.1.3.8) in the transfer of acetyl groups out of the mitochondria was investigated in rat liver its anti-enzyme. With a reconstructed system from normal rat liver (fed state), containing both the supernatant and the mitochondria, treatment of the supernatant with the antiserum reduced the acetylation of either sulfanilamide or p-toluidine by pyruvate to about 15% of the obtained by treatment of the supernatant with control serum. These drops in the rate of acetylation were completely reversed by addition of excess purified ATP citrate lyase. With mitochondria alone, it was found that the acetylation of these compounds was parallel to the amount of ATP citrate lyase added. Similar degrees of inhibition of the acetylation of p-toluidine by the antibody were obtained with preparations from the livers of fasted or diabetic rats. In addition, neither (−)- nor (+)-carnitine affected the acetylation rate under any conditions. From these findings, it was concluded that more than 80% of the extramitochondrical acetyl-CoA, derived from pyruvate via the mitochondria, is supplied through the ATP citrate lyase pathway in rat liver, even in the fasted or diabetic state." @default.
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- W1966929750 title "The role of ATP citrate lyase in the transfer of acetyl groups in rat liver" @default.
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- W1966929750 doi "https://doi.org/10.1016/0304-4165(68)90071-8" @default.
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