Copper catalyzed oxidation of ascorbate (vitamin C). Inhibitory effect of catalase, superoxide dismutase, serum proteins (ceruloplasmin, albumin, apotransferrin) and amino acids.
The inhibitory effect of catalase and superoxide dismutase on copper catalyzed oxidation of ascorbate is probably due to a binding of copper ions. Scavengers of hydroxyl ions and singlet oxygen had no effect on the ascorbate oxidation rate. Copper binding serum proteins reduced the oxidation rate; the order of effectiveness being: Ceruloplasmin greater than human albumin = bovine albumin greater than apotransferrin. The excellent protection obtained with catalase and ceruloplasmin is possibly due to a strong affinity for cuprous ions generated during the reaction. Cupric ion binding amino acids (His, Thr, Glu, Gln, Tyr) had considerably weaker protective effect than the proteins studied. Apparently they do not compete favorably with ascorbate for cupric ions.
D000596:Amino Acids / Q000494:pharmacology; D000818:Animals; D001205:Ascorbic Acid / Q000378:metabolism*; D001798:Blood Proteins / Q000494:pharmacology*; D002374:Catalase / Q000378:metabolism*; D002417:Cattle; D002570:Ceruloplasmin / Q000494:pharmacology; D003300:Copper / Q000378:metabolism*; D012709:Serum Albumin / Q000494:pharmacology; D013482:Superoxide Dismutase / Q000378:metabolism*; D014168:Transferrin / Q000494:pharmacology
D000596:Amino Acids; D001798:Blood Proteins; D012709:Serum Albumin; D014168:Transferrin; D003300:Copper; D002374:Catalase; D013482:Superoxide Dismutase; D002570:Ceruloplasmin; D001205:Ascorbic Acid