Purification and characterization of ceruloplasmin receptors.
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.
Omoto
E
E
Veterans Administration Medical Center, Jackson, MS.
Tavassoli
M
M
D000818:Animals; D001345:Autoradiography; D002462:Cell Membrane / Q000378:metabolism; D002570:Ceruloplasmin / Q000378:metabolism*; D002846:Chromatography, Affinity; D004591:Electrophoresis, Polyacrylamide Gel; D006026:Glycoside Hydrolases; D008099:Liver / Q000378:metabolism; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase; D008970:Molecular Weight; D051381:Rats; D011956:Receptors, Cell Surface / Q000302:isolation & purification*; D011971:Receptors, Immunologic; D018000:Receptors, Peptide
D011956:Receptors, Cell Surface; D011971:Receptors, Immunologic; D018000:Receptors, Peptide; C040519:ceruloplasmin receptor; D002570:Ceruloplasmin; D006026:Glycoside Hydrolases; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase