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Protein Thiyl Free Radicals Produced By Nitric Oxide and Nitric Oxide Donors

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The spin-trapping technique was used to study the radical intermediates produced by reaction of nitric oxide (*NO) and peroxynitrite with serum albumin and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Our results show that the major radical product induced by NO and by peroxynitrite with serum albumin and GAPDH was a thiyl radical. The same radical can be detected in the 'NO-transfer from S-nitroso albumin to low molecular weight thiols. Moreover, *NO or peroxynitrite treatment of GAPDH was able to induce NAD-dependent covalent modification of the enzyme in erythrocyte ghosts.

Affiliations: 1: Department of Cell Biology - Istituto Superiore di Sanità - V. Regina Elena 299 I-00161 Rome, Italy


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