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Updated: Jul 18, 2026

Characterizing Mammalian Zinc Transporters Using an In Vitro Zinc Transport Assay
Published on: June 2, 2023
Binding of zinc cations to human serum gamma-globulin
E E Babaeva1, U A Vorobyova, E A Denisova
1Laboratory of Cell-Cell Interactions, N. F. Gamaleya Institute of Epidemiology and Microbiology, Russian Academy of Medical Sciences, Moscow.
Abstract:
Binding of zinc cations to human serum gamma-globulin was studied by molecular ultrafiltration. The content of free metal in the filtrate was evaluated by reaction with o-phenanthroline. Conformation characteristics of the protein were determined by UV spectrophotometry. Our findings suggest that gamma-globulin molecule contains several zinc binding sites differing by corresponding constants and successively occupied with increase in the content of bound metal. The parameters of zinc binding correspond to those obtained in experiments with copper. Conformation status of protein with bound zinc differs significantly from that of protein with bound copper cations.
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