title: Human serum gamma-globulin binds copper cations.
abstract: 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.
authors.affiliation: Laboratory of Cell-to-Cell Interactions, N F Gamaleya Institute of Epidemiology and Microbiology.
authors.forename: E E
authors.initials: EE
authors.lastname: Babaeva
authors.forename: U A
authors.initials: UA
authors.lastname: Vorobyova
authors.forename: M S
authors.initials: MS
authors.lastname: Zharkova
authors.forename: S B
authors.initials: SB
authors.lastname: Cheknyov
mesh_terms: D001665:Binding Sites; D002412:Cations / Q000737:chemistry; D003300:Copper / Q000737:chemistry*; D006801:Humans; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet; D014462:Ultrafiltration; D005719:gamma-Globulins / Q000737:chemistry*
chemical_list: D002412:Cations; D005719:gamma-Globulins; D003300:Copper