BINDING OF HUMAN-SERUM FERRITIN TO CONCANAVALIN-A

A high proportion of the ferritin in normal serum binds to concanavalin A. Binding is prevented by the addition of α-D-methylglucoside to the reaction mixture. Ferritin in extracts of normal heart, liver and spleen or serum ferritin from patients with massive hepatic necrosis does not bind to concanavalin A. Isoelectric focusing of preparations of serum ferritin from patients with primary haemochromatosis shows that the ferritin fraction binding to concanavalin A consists, predominantly, of the more acidic isoferritins. These findings suggest that carbohydrate residues may be added to ferritin during its secretion into the plasma. Glycoslation may account for the heterogeneity of serum ferritin on isoelectric focusing. Direct release of intracellular ferritin from damaged tissue may be indicated by an increase in the proportion of circulating ferritin which does not bind to concanavalin A. Such an increase has been found in sera from patients with iron overload.