Abstract
WE have investigated the specific co-glyoxalase action of glutathione, discovered by Lohmann1. Giraviius and Heyfetz2 have shown that the spontaneous combination of glutathione and methyl glyoxal in aqueous solution leads to a state of equilibrium; formation and dissociation of the compound proceed, in not too acid solution, with great rapidity. The dependence of the velocity of the enzymic reaction on the initial concentrations of glutathione and methyl glyoxal (Platt and Schroeder3) and of their compound (unpublished work of ours) leads to the conclusion that of the three substances—free glutathione, free methyl glyoxal, and the compound— it is the latter that is the true substrate of glyoxalase action (though one of the other two may also be playing a part).
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References
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J. biol. Chem., 104, 281 ; 1934.
J. Biochem. (Tokyo), 16, 317 ; 1932.
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GIRAVIIUS, J., HEYFETZ, P. Mechanism of Glyoxalase Activation by Glutathione. Nature 136, 645–646 (1935). https://doi.org/10.1038/136645a0
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DOI: https://doi.org/10.1038/136645a0
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