Mutarotase equilibrium exchange kinetics studied by 13C-NMR
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P W Kuchel1, B T Bulliman, B E Chapman
1Department of Biochemistry, University of Sydney, NSW, Australia.
Biophysical Chemistry
|October 1, 1988
Abstract:
The rates of exchange between the alpha- and beta-anomers of D-[1-13C]glucose, at equilibrium catalyzed by porcine kidney mutarotase (EC 5.1.3.3), were measured using 13C-NMR spin-transfer procedures. This entailed inversion-transfer and saturation-transfer experiments, and two-dimensional exchange spectroscopy (2D EXSY). The concentration and temperature dependences of the fluxes were studied; equilibrium exchange Michaelis constants, and the activation energy of the catalyzed reaction were thereby measured.