Add time:08/03/2019         Source:sciencedirect.com

Oxidation of p,p′-biphenol with horseradish peroxidase (HRP)-hydrogen peroxide in the presence of bovine serum albumin or with bone marrow cell homogenate-hydrogen peroxide resulted in the formation of reactive products that conjugate with protein. Glutathione prevented the protein binding. Glutathione readily reacted with p,p′-biphenoquinone, the principal oxidation product of p,p′-biphenol in the HRP-hydrogen peroxide system and resulted in the formation of several glutathione conjugates, p,p′-biphenol and small amounts of oxidized glutathione. The major glutathione conjugate was identified as 3-(glutathion-S-yl)-p,p′-biphenol by high field nuclear magnetic resonance and fast atom bombardment mass spectrometry. The same conjugate was formed in the bone marrow homogenate-hydrogen peroxide system. p,p′-Biphenoquinone reduction by glutathione to p,p′-biphenol without glutathione oxidation was explained by the rapid reduction of p,p′-biphenoquinone by 3-(glutathion-S-yl)-p,p′-biphenol.

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