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Site specificity of iron removal from transferrin by α-ketohydroxypyridine chelators

Authors
Journal
FEBS Letters
0014-5793
Publisher
Wiley Blackwell (John Wiley & Sons)
Publication Date
Volume
189
Issue
1
Identifiers
DOI: 10.1016/0014-5793(85)80859-0

Abstract

Abstract The site specificity of the removal of iron from diferric human transferrin, at pH 7.4, by two α-ketohydroxypyridine chelators, 1,2-dimethyl-3-hydroxypyrid-4-one (L 1) and mimosine, has been investigated using urea-polyacrylamide gel electrophoresis. Chelator L 1 removes iron preferentially from the C-terminal site whereas mimosine shows a small preference for iron in the N-terminal site. The removal of iron has also been followed spectrophotometrically and by monitoring the loss of 59Fe from [ 59Fe]transferrin. Both chelators are able to remove iron completely from diferric transferrin without additional mediators or reducing agents. Transferrin Iron mobilisation Site specificity α-Ketohydroxypyridine chelators Mimosine

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