Purification and characterization of ceruloplasmin receptors

Abstract

Membrane receptors for ceruloplasmin were isolated by affinity chromatography using CP bound to CNBr-activated Sepharose 4B. The receptor was obtained in the form of a single sharp peak which when collected, concentrated and run on SDS-PAGE provided a single band with a molecular weight of 35,000. Treatment with endoglycosidase F reduced this molecular weight by 3%. It is concluded that ceruloplasmin receptors in this cell system is a membrane protein containing 3% carbohydrate with a total molecular weight of 35,000. It is possible that this is a monomer of a higher molecular weight protein.