Calcium ion binding to clinically relevant chemical modifications of human serum albumin.
作者： H Vorum , K Fisker , M Otagiri , A O Pedersen , U Kragh-Hansen
DOI: 10.1093/CLINCHEM/41.11.1654
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摘要: Calcium binding to glycated, penicilloylated, acetylated, and normal defatted human serum albumin as well mercapt- nonmercaptalbumin was studied by equilibrium dialysis of radioactive Ca2+. Binding quantified five Scatchard constants [ni = 1, (i 1-4) n5 10]. Glycation resulted in increased k1- k2-values unchanged k3-k5-values, whereas penicilloylation all association constants. The increments were greater the more pronounced modification, enhancements caused were, for same degree than those produced glycation. In contrast, acetylation acetylsalicylate did not affect calcium binding. Likewise, same, a finding showing that thiol group cysteine 34 is important D-Glucose penicillin G are known react with lysine residues albumin, enhancement resulting from glycation or probably brought about unspecific electrostatic effects, possibly supplemented conformational changes protein molecule. relative importance three domains discussed.
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