Abstract
The interaction of Cu(II) and human serum albumin (HSA) or bovine serum albumin (BSA) at physiological pH is studied by equilibrium dialysis. The successive stability constants are obtained by non-linear least square methods fitting Bjerrum formula. For both the Cu(II)-HSA and Cu(II)-BSA systems, the order of magnitude of K1 and K2 was found to be ≈104 mol−1· dm3. There are about twenty stoichiometry binding sites found in one HSA or BSA molecule. They can be divided into two or three sets. Results of equilibrium dialysis experiments suggest that there exists one strong metal binding site in both Cu(II)-HSA and Cu (II)-BSA. It is the imidazol group nitrogen atoms of His3 that are primarily concerned with copper binding site. After reaching dialysis equilibrium, there is the interaction among the different binding sites, the values ofK all deviate from the simple statistical effect except forK 1 and K2 in both Cu(II)-HSA and Cu(II)-BSA systems, and the positive cooperative effect is found.
Similar content being viewed by others
References
Zhou, Y. Q., Wang, Y. W., Hu, X. Y.el al., Equilibrium dialysis of metal-serum albumin, I. Successive stability constants of Zn(II)-serum albumin and the Zn2+-induced cross-linking self-association,Biophysical Chemistry, 1994, 51: 81.
Zhou, Y. Q., Tai, J. Z., Liang, H.et al., Structure studies on metal-serum albumin (IV)—A novel hypochromic effect in Ni(II)-HSA and Ni(II)-BSA,Chemical Journal of Chinese Universities (in Chinese), 1996, 17(9): 1331.
Shen, P. W., Zhou, Y. Q., Wang, S. Y.et al., Structural studies on metal-serum albumin, I. An ultraviolet spectroscopic study of copper (II)-human serum albumin complexes,Inorg. Chim. Acta, 1990, 169(2): 161.
Zhou, Y. Q., Liang, H., Shen, P. W.et al., Structural studies on metal-serum albumin VI. Structure of the Cu(II) and Ni(II) metal centre in HSA and BSA nearby isoionic point,Journal of Inorganic Chemistry (in Chinese), 1992, 8(4): 382.
Adad, C., Trueba, M., Macaralla, J. M.et al., Structural studies of copper protein systems by dilatometry, differential refractometry, and viscometry,An. Quim., Ser. A, 1980, 76(2): 171.
Korsenoer, V. M., Oratz, M., Rothchild, M. A.,Albumin Structure Functions and Uses, Oxford: Pergamon Press, 1977.
Masuoka, J., Hegenauer, J., Van Dyke, B. R.et al., Intrinsic stoichiometric equilibrium constants for the binding of zinc (II) to the high affinity site of serum albumin,J. Biol. Chem., 1993, 268 (29): 21 533.
Wells, J. W.,In Receptor-ligand Interactions (ed Hulme, E. C.), Oxford: Oxford University Press, 1992.
Edsall, J. T., Felsenfeld, G., Goodman, D. S.et al., The association of imidazole with the ions of zinc and cupric copper,J. Am. Chem. Soc., 1954, 76: 3054.
Putnam, F. W.,The Plasma Protein Structure, Functions and Genetic Control, 2nd ed., New York: Academic Press, 1975.
Rubin, M. M., Changeux, I. P., On the nature of allosteric transitions: Implications of non-exclusive ligand binding,J. Mol. Biol., 1966, 21(2): 265.
Author information
Authors and Affiliations
About this article
Cite this article
Liang, H., Xin, B., Wang, X. et al. Equilibrium dialysis study on the interaction between Cu(II) and HSA or BSA. Chin. Sci. Bull. 43, 404–409 (1998). https://doi.org/10.1007/BF02883720
Received:
Issue Date:
DOI: https://doi.org/10.1007/BF02883720