A newly identified iron binding protein in duodenal mucosa of rats. Purification and characterization of mobilferrin.
An iron binding protein with an approximate molecular mass of 56,000 daltons was purified to homogeneity from homogenates of rat duodenal mucosa. The protein was biochemically and immunologically distinct from transferrin and ferritin and competitively bound cobalt, copper, zinc, and lead. Each molecule bound one molecule of iron with a Kd of 9 X 10(-5). Dissociation of iron and the protein was accelerated at acid pH. Using an immunogold method, the protein was identified in the apical cytoplasm of proximal small intestinal cells and was not observed elsewhere in the intestinal mucosa and in other body organs. It was named mobilferrin from its city of origin and to differentiate it from other previously identified iron binding proteins.
Conrad
M E
ME
Department of Medicine, University of South Alabama, Mobile 36688.
Umbreit
J N
JN
Moore
E G
EG
Peterson
R D
RD
Jones
M B
MB
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000032:analysis / Q000302:isolation & purification / Q000378:metabolism*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004386:Duodenum / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D007150:Immunohistochemistry; D007413:Intestinal Mucosa / Q000166:cytology / Q000378:metabolism*; D007501:Iron / Q000378:metabolism*; D007700:Kinetics; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains
D000596:Amino Acids; D002352:Carrier Proteins; D007501:Iron