Site specificity of iron removal from transferrin by alpha-ketohydroxypyridine chelators.
The site specificity of the removal of iron from diferric human transferrin, at pH 7.4, by two alpha-ketohydroxypyridine chelators, 1,2-dimethyl-3-hydroxypyrid-4-one (L1) and mimosine, has been investigated using urea-polyacrylamide gel electrophoresis. Chelator L1 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.
D000077543:Deferiprone; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D007501:Iron / Q000378:metabolism*; D008898:Mimosine / Q000494:pharmacology*; D011728:Pyridones / Q000494:pharmacology*; D013997:Time Factors; D014168:Transferrin / Q000378:metabolism*
D011728:Pyridones; D014168:Transferrin; D000077543:Deferiprone; D008898:Mimosine; D007501:Iron