Prothrombotic Consequences of the Oxidation of Fibrinogen and their Inhibition by Aspirin.

Oxidant stress leads to covalent oxidative modification of several plasma proteins, chief among which is fibrinogen. Aspirin can nonenzymatically acetylate fibrinogen's lysine residues, the functional groups most susceptible to oxidative modification. Because oxidation of fibrinogen may occur in the atheromatous environment, we studied the effects of oxidative modification on fibrinogen function and the consequences of acetylation by aspirin on fibrinogen's susceptibility to oxidation and functional properties.

Detection of S-nitrosothiols and other nitric oxide derivatives by photolysis-chemiluminescence spectrometry.

We have developed a method for the detection of biologically relevant derivatives of NO. that couples photolysis to chemiluminescence. S-Nitrosothiols, N-nitroso-L-tryptophan, and iron-nitrosyl derivatives can all be detected by this methodology, and these derivatives can be distinguished from free NO.