Hemolysis and lodination of Erythrocyte Components by a Myeloperoxidase - mediated System
نویسنده
چکیده
Erythrocytes are hemolyzed by myeloperand triiodothyronine-dependent, but not oxidase, an H203-generating system (gluin the chloride-dependent, systems. Hemocose + glucose oxidase; hypoxanthine + lysis is inhibited by the peroxidase inxanthine oxidase) and an oxidizable cohibitors, azide and cyanide, and by catafactor (chloride, iodide, thyroxine, tnlase and is stimulated by superoxide iodothyronine) . The combined effect of dismutase when the xanthine oxidase syschloride and either iodide or the thyroid tern is employed as the source of H202. hormones is greater than additive. MyeHemolysis by the iodide-dependent sysloperoxidase can be replaced by lactotern is associated with the iodination of peroxidase in the iodide-, thyroxineerythrocyte components.
منابع مشابه
Hemolysis and iodination of erythrocyte components by a myeloperoxidase-mediated system.
Erythrocytes are hemolyzed by myeloperoxidase, an H2O2-generating system (glucose + glucose oxidase; hypoxanthine + xanthine oxidase) and an oxidizable cofactor (chloride, iodide, thyroxine, triiodothyronine). The combined effect of chloride and either iodide or the thyroid hormones is greater than additive. Myeloperoxidase can be replaced by lactoperoxidase in the iodide-, thyroxine and triiod...
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