Effect of Nitrosylated Albumin in the Isolated Rabbit Heart
Recent evidence suggests that compounds containing a free sulfhydryl group can react with nitric oxide (NO) under physiological conditions. Both the detection of S-nitroso compounds, especially S-nitrosylated proteins (Stamler et al. 1991,1992a, b; Keaney et al. 1993) and that of dinitrosyl-ferrous iron complexes with protein-bound and with low molecular weight thiols (Mülsch et al. 1991; Vanin et al. 1993; Busse et al. 1993) have been reported. It is convincible from the preponderance of evidence that endothelium-derived relaxing factor first observed by Furchgott and Zawadzki (1980) is NO, being the immediate product of both the constitutive and inducible NO synthase in intact endothelial cells, macrophages, and other cells. However, the fate of NO after its generation is still in part an open question. As pointed out by Busse et al. (1993) in a recent review it is hard to understand why the reaction pathway of (endothelium-derived) NO should be restricted to inactivation by oxygen or by soluble guanylyl cyclase. The NO radical is in principle capable of oxidizing many important molecules such as compounds containing thiol groups, heme groups, iron-sulfur centers, (primary) amines, and unsaturated fatty acyl groups (via oxides of nitrogen). Most part of the information is derived from in vitro experiments. S-Nitrosocysteine has, for instance, been reported to more closely resemble the vasorelaxant properties of endothelium-derived relaxing factor than NO (Myers et al. 1990).
KeywordsNitric Oxide Human Serum Albumin Coronary Flow Isolate Rabbit Heart Postcolumn Derivatization
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