Purification and characterization of the intestinal promoter of iron(3+)-transferrin formation

The nonceruloplasmin enzyme located in the intestinal mucosa which promotes the incorporation of iron into transferrin has been resolved into a small, heat-stable component and a heat-labile protein component. The small, heat-stable component was purified from the high-speed supernatant of intestina...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 1981-01, Vol.20 (2), p.319-324
Main Authors: Topham, Richard W, Woodruff, James H, Walker, Mark C
Format: Article
Language:English
Subjects:
Allopurinol - pharmacology
Animals
Duodenum - enzymology
Intestinal Mucosa - enzymology
Iron - metabolism
Kinetics
Molecular Weight
Rabbits
Spectrometry, Fluorescence
Spectrophotometry
Superoxides - metabolism
Transferrin - metabolism
Xanthine Oxidase - isolation & purification
Xanthine Oxidase - metabolism
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The nonceruloplasmin enzyme located in the intestinal mucosa which promotes the incorporation of iron into transferrin has been resolved into a small, heat-stable component and a heat-labile protein component. The small, heat-stable component was purified from the high-speed supernatant of intestinal mucosal homogenates by ion-exchange chromatography and gel filtration and identified as xanthine. The heat labile protein component was purified from the high-speed supernatant of intestinal mucosal homogenates by heat treatment, gel filtration, and ion-exchange chromatography. The physical, spectral, and kinetic properties of the heat-labile protein component strongly suggest that it is xanthine oxidase. By promotion of the oxidation and incorporation of iron into transferrin, intestinal xanthine oxidase could perform a similar function in iron absorption as ceruloplasmin serves in the mobilization of iron from liver stores.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00505a014