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Physiological zinc-binding proteins of medium molecular weight in the rat gut

Published online by Cambridge University Press:  09 March 2007

Malcolm J. Jackson ,
Daphne Holt ,
Michael Webb  and
Nicholas D. Carter
Malcolm J. Jackson
Affiliation:
Department of Medicine, University of Liverpool, PO Box 147, Liverpool L69 3BX
Daphne Holt
Affiliation:
Toxicology Unit, MRC Laboratories, Woodmansterne Road, Carshalton, Surrey SM5 4EF
Michael Webb
Affiliation:
Toxicology Unit, MRC Laboratories, Woodmansterne Road, Carshalton, Surrey SM5 4EF
Nicholas D. Carter
Affiliation:
Department of Child Health, St. George's Hospital Medical School, Cranmer Terrace, London SW17
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Abstract

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1. Gel filtration on Sephadex G 75 was used to separate the medium-molecular-weight zinc-binding proteins from the soluble fractions from the duodenal and jejuno-ileal segments of the rat gut at 30 min after the intragastric administration of a tracer dose of 65Zn. These proteins were resolved by ion-exchange chromatography on DEAE cellulose.

2. In both the duodenum and jejuno-ileal segment an appreciable fraction of the total soluble Zn was bound in a protein fraction that resembled metallothionein [MT] in its behaviour on gel filtration. These fractions, however, were not homogeneous, but contained several medium-molecular-weight Zn-binding proteins. In the duodenum, but not in the jejuno-ileal segment, two ofthese proteins appeared to be the isometallothioneins, ZnMT-I and ZnMT-11.

3. These results suggest a possible role for MT in the binding of newly-absorbed Zn in the duodenal mucosal cells. They also show that gel filtration alone is insufficient for the identification of MT in the intestine.

Type
Papers on General Nutrition
Information
British Journal of Nutrition , Volume 55 , Issue 2 , March 1986 , pp. 369 - 377
Copyright
Copyright © The Nutrition Society 1986

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