[Interaction of divalent metal ions with human serum albumin].
ESR study was carried out of the interaction between Zn2+, Cu2+, Ca2+, Mg2+ ions and human serum albumin (HSA) in the presence of Mn2+ ions which depends on pH. Competitive binding of these ions with "manganese-binding" sites of albumin was shown to depend on pH. An analysis of concentration dependence of binding these ions with human serum albumin confirmed earlier supposition about the nature of the binding sites of Mn2+ ions with HSA.
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D001667:Binding, Competitive; D002352:Carrier Proteins / Q000378:metabolism; D002413:Cations, Divalent / Q000378:metabolism; D006801:Humans; D008345:Manganese / Q000097:blood / Q000378:metabolism; D008670:Metals / Q000097:blood / Q000378:metabolism*; D012709:Serum Albumin / Q000378:metabolism*
D002352:Carrier Proteins; D002413:Cations, Divalent; D008670:Metals; D012709:Serum Albumin; D008345:Manganese
Vzaimodeĭstvie dvukhvalentnykh ionov metallov s syvorotochnym al'buminom cheloveka.