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- W2093232317 abstract "Initial rate studies at pH 7.6 with three aldehydes, product inhibition patterns with NADH and dead-end inhibition with adenosine diphosphoribose show that the kinetic mechanism of glyceraldehyde-3-phosphate dehydrogenase from rabbit muscle cannot be ordered, and support an enzyme-substitution mechanism. Deviations from Michaelis-Menten behaviour are consistent with negative interactions in the binding of NAD+ and instability of the species E(NAD)3 and E(NAD)4. Inhibition with large concentrations of phosphate and arsenate indicates competition for a binding site for glyceraldehyde 3-phosphate, and is not found with glyceraldehyde as substrate." @default.
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- W2093232317 date "1978-01-01" @default.
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- W2093232317 title "Kinetic Studies of Glyceraldehyde-3-Phosphate Dehydrogenase from Rabbit Muscle" @default.
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- W2093232317 doi "https://doi.org/10.1111/j.1432-1033.1978.tb12042.x" @default.
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