Hemin-induced lysis of rat erythrocytes. Protective action of ceruloplasmin and different serum albumins.
Hemin-induced lysis of rat erythrocytes is markedly reduced by ceruloplasmin (human) and serum albumins from different species, the order of effectiveness beings: bovine albumin approximately equal to ceruloplasmin greater than human albumin approximately equal to dog albumin greater than apotransferrin (human). Although the proteins studied had hemin binding capacity, the best protective agents, ceruloplasmin and bovine albumin, did bind hemin less strongly than human and dog albumin. The results suggest the existence of another protective mechanism, possibly involving an interaction between erythrocyte membranes and serum proteins.
D000818:Animals; D002110:Caffeine / Q000494:pharmacology; D002417:Cattle; D002570:Ceruloplasmin / Q000494:pharmacology*; D004285:Dogs; D004912:Erythrocytes / Q000502:physiology*; D006418:Heme / Q000494:pharmacology*; D006461:Hemolysis / Q000187:drug effects*; D006801:Humans; D007700:Kinetics; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains; D012709:Serum Albumin / Q000494:pharmacology*; D013045:Species Specificity; D013053:Spectrophotometry
D012709:Serum Albumin; D002110:Caffeine; D006418:Heme; D002570:Ceruloplasmin