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- W2009580652 abstract "Interactions of human α-lactalbumin with Pb2+ and Hg2+ were studied by intrinsic protein fluorescence. Lead ions bind to the strong Ca2+ binding site of α-lactalbumin (association constant Kass≈︁2×106 M-1) with concomitant spectral changes which are similar to those induced by the binding of Ca2+. Pb2+ also binds to the strong Zn2+ site with Kass≈︁105 M-1 and some secondary binding site(s) (which probably contain histidine residues) with apparent Kass≈︁104 M-1, causing pronounced aggregation of the protein. Mercury ions bind to α-lactalbumin at the primary Zn2+ sites with Kass≈︁(1-4)×104 M-1, although the stoichiometry of the binding depends on the conformational state of the protein. Secondary Hg2+ binding sites were suggested to contain histidines, while the strong Hg2+ site contains carboxylates in the coordination sphere and seems to coincide with the strong Zn2+ site. The binding of both Pb2+ and Hg2+ decreases the thermal stability of the Ca2+-loaded protein and in some conditions causes pronounced protein aggregation." @default.
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- W2009580652 date "1996-08-01" @default.
- W2009580652 modified "2023-10-18" @default.
- W2009580652 title "Pb2 and Hg2 binding to α-lactalbumin" @default.
- W2009580652 doi "https://doi.org/10.1080/15216549600201452" @default.
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