Biomedical subjects

M S Zharkova

Publications and source records attributed to M S Zharkova.

3 recordsLinked to original sources

PubMed2006

Human serum gamma-globulin binds copper cations.

Binding of copper cations to human serum gamma-globulin was studied using molecular ultrafiltration. The content of free metal in the filtrate was evaluated by the reaction with sodium diethyldithiocarbamate. Conformation characteristics of the protein were evaluated by UV spectrophotometry. gamma-Globulin molecule has several copper-binding sites differing by binding constants and filled one-by-one as the content of bound metal increased.

Binding Sites↗

PubMed2005

Formation of supramolecular aggregations of gamma-globulin as a metal-dependent process.

The presence of copper cations in the solution of human serum gamma-globulin induced the formation of supramolecular forms of the protein. The intensity of this reaction increased with increasing copper concentration. The mechanisms of g-globulin aggregate formation under normal conditions and the possible role of bivalent metal cations in the regulation of protein effector functions are discussed.

Cations, Divalent↗

PubMed2005

Biphasic interaction of gamma-globulin with copper cations.

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.

Cations↗