Cheknev S B, Babaeva E E, Zharkova M S
Laboratory of Cell-Cell Interactions, NF Gamaleya Institute of Epidemiology and Microbiology, Russian Academy of Medical Sciences, Moscow.
Bull Exp Biol Med. 2005 May;139(5):572-5. doi: 10.1007/s10517-005-0348-5.
Interactions of human serum gamma-globulin with copper cations in solution were studied by differential ultraviolet spectrophotometry. Copper in supraphysiological concentrations increases optical density of protein solution, reflecting the effect of gamma-globulin saturation with metal. In physiological and lower concentrations of copper cations we observed hypochromia in the protein absorption spectrum. Conformational changes in g-globulin molecule during interactions with copper by the surface and intramolecular binding sites and possible role of bivalent metal cations in the maintenance of certain conformations of immunoactive serum proteins are discussed.
采用差示紫外分光光度法研究了人血清γ-球蛋白与溶液中铜离子的相互作用。超生理浓度的铜会增加蛋白质溶液的光密度，这反映了γ-球蛋白被金属饱和的效应。在生理浓度及更低浓度的铜离子条件下，我们观察到蛋白质吸收光谱出现减色现象。讨论了γ-球蛋白分子在通过表面和分子内结合位点与铜相互作用过程中的构象变化，以及二价金属阳离子在维持免疫活性血清蛋白特定构象方面可能发挥的作用。
