Kinetic Studies of Glyceraldehyde‐3‐Phosphate Dehydrogenase from Rabbit Muscle
1978; Wiley; Volume: 82; Issue: 2 Linguagem: Inglês
10.1111/j.1432-1033.1978.tb12042.x
ISSN1432-1033
AutoresJean‐Claude Meunier, Keith Dalziel,
Tópico(s)Mass Spectrometry Techniques and Applications
ResumoInitial 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.
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