Apotransferrin proton dissociation and interactions with hydrogencarbonate in neutral media
作者： Louisa Bellounis , Rowchanak Pakdaman , Jean Michel El Hage Chahine
DOI: 10.1002/(SICI)1099-1395(199602)9:2<111::AID-POC761>3.0.CO;2-4
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摘要: A spectrofluorimetric titration analysis of the proton dissociation and interactions human serum transferrin with hydrogencarbonate was performed at pH 7·0–9·0. Apotransferrin loses a single probably per binding site Ka = (6·80 ± 0·35) × 10−9M. This is independent concentration. does not interact CO32−. However, it interacts two HCO3−, exhibiting different affinity constants; constant presumably for C-site KC (4·40 0·15) 10−3M that N-site KN (3·60 0·30) 10−2M. These are occur unprotonated protonated apotransferrin species same low affinities. Such affinities induced by ionic involving side chain arginine residues in each sites. As dissociation, can one other side-chains amino acid these
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