Rabbit serum alpha-2-macroglobulin binds to liver ferritin: association causes a heterogeneity of ferritin molecules.

Rabbit liver ferritin is unusual since it forms two discrete electrophoretic bands at the beta position of molecular dimers (Santambrogio & Massover, 1987). The present studies have sought to identify the nature of a 170 kDa non-ferritin polypeptide that is uniquely present in the larger beta band. Ultrastructural, immunological and biochemical results all indicate that this polypeptide is a subunit of the plasma protein. alpha-2-macroglobulin. Experimental results show that rabbit serum alpha-2-macroglobulin will bind liver ferritin, and this association induces the de novo formation of the larger beta band. These results thus demonstrate that molecular heterogeneity of ferritin can be caused by its association with a non-ferritin protein. We conclude that alpha-2-macroglobulin is a binder of rabbit tissue ferritin in the circulation; this binding could provide additional means for the receptor-mediated uptake of circulating ferritin.