Isolation of a porcine hepatic ferritin receptor.
1. A ferritin receptor has been isolated from porcine liver and has been partially purified using affinity chromatography. 2. A binding assay has been developed which utilizes a hepatic ferritin receptor coupled to a microparticulate support which facilitates the separation of bound and free ligand. 3. An affinity constant of 2.9 x 10(9) mol-1 litre was determined for the purified hepatic ferritin receptor. 4. The molecular weight of the receptor was estimated to be approximately 53,000 by gel electrophoresis. 5. Binding of ferritin to the insolubilized receptor was unaffected by a 100-fold excess of bovine albumin, porcine and human transferrin, and human asialo-orosomucoid. 6. Binding was specific for porcine ferritin with no demonstrable binding of rat or human ferritin.
Adams
P C
PC
Department of Medicine, University of Queensland, Royal Brisbane Hospital, Australia.
Mack
U
U
Powell
L W
LW
Halliday
J W
JW
D000818:Animals; D005293:Ferritins / Q000378:metabolism; D066298:In Vitro Techniques; D033862:Iron-Binding Proteins; D007700:Kinetics; D008099:Liver / Q000378:metabolism*; D008970:Molecular Weight; D011956:Receptors, Cell Surface / Q000302:isolation & purification* / Q000378:metabolism; D013552:Swine
D033862:Iron-Binding Proteins; D011956:Receptors, Cell Surface; C027293:ferritin receptor; D005293:Ferritins