Immuno-Enzyme Analysis of the g-Globulin which Had Bound Metal Ions, at the Low Samples Concentrations
Immuno-enzyme analysis of the human serum g-globulin modified by copper or zinc ions binding was provided with using low samples concentrations and specific anti-human IgG (H+L) antibodies. It has been shown that the dynamics of a solid phase monolayer formation was different between the tested and control proteins. The g-globulin that bound zinc has formed the protein monolayer earlier than its control, whereas g-globulin that bound copper has formed but has not saturated the protein monolayer. Reaction with the specific antibodies was higher for the zinc-modified g-globulin and was significantly lower for the copper-modified g-globulin than for the respective controls used. The data obtained allow to suggest that the primary transformations of the g-globulin bound copper or zinc ions were associated with changes in the Fc fragments of the molecule. The possibilities to use the results in theory of the metal-protein interactions as well as in the clinics were discussed.