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Steady-state parameters of an enzyme from n.m.r. spin transfer with thermal variation
1Department of Biochemistry, University of Sydney, N.S.W., Australia.
The Biochemical Journal
|May 15, 1987
Abstract:
N.m.r. spin-exchange analysis of enzymic reactions at chemical equilibrium is akin to radioactive-tracer-exchange analysis; unidirectional flux rates are obtained for the overall reaction. These data, by themselves, are not sufficient to define the values of all the individual rate constants or steady-state parameters. However, it is shown that, by measuring the dependence of the exchange rate constants on solute concentration and temperature, the individual rate constants, and hence the steady-state parameters, can be obtained for a simple enzyme system.