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-G...

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Bibliographic Details
Published in:Bulletin of experimental biology and medicine 2006-01, Vol.141 (1), p.53-56
Main Authors: Babaeva, E E, Vorobyova, U A, Zharkova, M S, Cheknyov, S B
Format: Article
Language:English
Subjects:
Binding Sites
Cations - chemistry
Copper - chemistry
gamma-Globulins - chemistry
Humans
Protein Conformation
Spectrophotometry, Ultraviolet
Ultrafiltration
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Summary: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.
ISSN:0007-4888
1573-8221
DOI:10.1007/s10517-006-0092-5