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. 1982 Jul 15;27(2):197-203.
doi: 10.1016/0049-3848(82)90199-2.

The kinetic mechanism of glutathione peroxidase from human platelets

J I Martínez, R D García, A M Galarza

The kinetic mechanism of glutathione peroxidase from human platelets

J I Martínez et al. Thromb Res. .

Abstract

Human platelet glutathione peroxidase (GSH-Px) exhibits a ping-pong type kinetic mechanism. Peroxide changes the redox state of the enzyme and renders it highly stable against attack by alkylating agents. Peroxide seems also to act as a positive homotropic modulator modifying the allosteric kinetics of the enzyme. The combination of these two mechanisms accelerates response against peroxides. This finding reassesses importance of GSH-Px for the platelet protection.

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