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 mole...

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Veröffentlicht in:The Journal of biological chemistry 1990-03, Vol.265 (9), p.5273-5279
Hauptverfasser: CONRAD, M. E, UMBREIT, J. N, MOORE, E. G, PETERSON, R. D. A, JONES, M. B
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container_end_page 5279
container_issue 9
container_start_page 5273
container_title The Journal of biological chemistry
container_volume 265
creator CONRAD, M. E
UMBREIT, J. N
MOORE, E. G
PETERSON, R. D. A
JONES, M. B
description 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.
doi_str_mv 10.1016/S0021-9258(19)34117-1
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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. 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B</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A newly identified iron binding protein in duodenal mucosa of rats. Purification and characterization of mobilferrin</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1990-03-25</date><risdate>1990</risdate><volume>265</volume><issue>9</issue><spage>5273</spage><epage>5279</epage><pages>5273-5279</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>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. 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source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Amino Acids - analysis
Analytical, structural and metabolic biochemistry
Animals
Binding and carrier proteins
Biological and medical sciences
Carrier Proteins - analysis
Carrier Proteins - isolation & purification
Carrier Proteins - metabolism
Chromatography, Gel
Chromatography, Ion Exchange
duodenum
Duodenum - metabolism
Electrophoresis, Polyacrylamide Gel
Fundamental and applied biological sciences. Psychology
Immunohistochemistry
Intestinal Mucosa - cytology
Intestinal Mucosa - metabolism
Iron - metabolism
Kinetics
mobilferrin
Molecular Weight
mucosa
Proteins
Rats
Rats, Inbred Strains
title A newly identified iron binding protein in duodenal mucosa of rats. Purification and characterization of mobilferrin
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