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- W2036884534 abstract "Succinyl-CoA: 3-ketoacid CoA-transferase (EC 2.8.3.5) activity was demonstrated in the brain of man, rat, mouse, guinea pig, and pigeon, but not of the dog, calf, and pig. In contrast to the enzyme from heart tissue, the brain enzyme was a particulate protein which sedimented with the mitochondrial fraction. The protein could be solubilized in 0.3% deoxycholate, or by freezing and thawing, and fractional salt and acid precipitation, and DEAE-cellulose chromatography yielded a 300-fold purification of the rat brain enzyme. Double reciprocal plots of one substrate vs velocity at several concentrations of the second substrate resulted in parallel lines which suggested a “ping-pong” mechanism as has been described for the pig heart enzyme. The Km values for succinate, acetoacetate, and succinyl CoA were 3.9 × 10−2, 2.9 × 10−4, and 6.7 × 10−4m, respectively. In the rat, the thermal lability, acrylamide gel electrophoretic mobility, and substrate specificity were essentially the same for the enzymes obtained from either heart, brain, or kidney. These findings support the suggested physiological role for the enzyme in ketone oxidation in central nervous tissue." @default.
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- W2036884534 date "1972-02-01" @default.
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- W2036884534 title "CoA transferase in the brain and other mammalian tissues" @default.
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- W2036884534 doi "https://doi.org/10.1016/0003-9861(72)90155-5" @default.
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