@article{ref1,
title="Estimation of kinetic parameters in the inactivation of an enzyme by a suicide substrate",
journal="Biochimica et biophysica acta",
year="1991",
author="Funaki, T. and Takanohashi, Y. and Fukazawa, H. and Kuruma, I.",
volume="1078",
number="1",
pages="43-46",
abstract="A method was developed to estimate the extended Michaelis constant and maximum velocity of a suicide substrate from the time-course of remaining enzyme activity with the use of simulation data calculated from the representative kinetic model for a suicide substrate proposed by Walsh et al. (Walsh, C., Cromartie, T., Marcotte, P. and Spencer, R. (1978) Methods Enzymol. 53, 437-448). For this purpose an analytical equation for the time-course of remaining enzyme activity, based on the suicide kinetic model, was derived by the steady-state method reported by Tatsunami et al. (Tatsunami, S., Yago, N. and Hosoe, M. (1981) Biochim. Biophys. Acta 662, 226-235). The accuracy of this analytical solution was proved by comparing the result with the exact solution obtained by numerical computation. A method was also developed to estimate the most important factor for a suicide substrate, the partition ratio, from the time-course of remaining enzyme activity.<p /><p>Language: en</p>",
language="en",
issn="0006-3002",
doi="10.1016/0167-4838(91)90090-m",
url="http://dx.doi.org/10.1016/0167-4838(91)90090-m"
}