Author:
Davis K. A.,Williams G. R.
Abstract
The 200-fold purification of glyoxaiase I (EC 4.4.1.5) from calf liver is described. This enzyme exhibits two marked anomalies in its kinetic behavior. There is an initial lag phase of a few seconds, and the plot of velocity versus enzyme concentration is nonlinear, reaching a plateau value. These features are correlated with the kinetics of formation of the hemimercaptal of glutathione and methylglyoxal, suggesting that this adduct is the true substrate of glyoxaiase I.
Publisher
Canadian Science Publishing
Cited by
33 articles.
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