Document Detail


[Immobilization of the glutathione by the complementary coordination binding].
MedLine Citation:
PMID:  22332356     Owner:  NLM     Status:  In-Process    
Abstract/OtherAbstract:
A simple method for immobilization of biologically imporant molecules with many functional fragments by selective binding of their thiogroups with the surface caroxyl groups by cadmium ions was proposed. Biofunctional properties of these structures were studied by surface plasmon resonance method on the model of the glutathione (GSH), which was immobilized by means of mixed (a:b form 1:100 o 1:700) thiol monolayers with terminal groups of the methyl/hydroxyl (b) and carboxyl (a) type. The maintenance of the biofunctional conformation ofglutathione-S-transferase (GST) after its interaction with GSH was checked by the use of specific anti-GST antibodies. It was shown that CH3 matrix has considerable non-specific binding and is not suitable for the formation of the biofunctional GST layer. At the same time OH-based structures demonstrate specific interaction GST-anti-GST, the stoichiometry of which corresponds to the bidentate binding. Considered simple method of the immobilization can be used to create the functional surface architectures in the analyticasl biochemistry and chemical analysis.
Authors:
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Publication Detail:
Type:  English Abstract; Journal Article    
Journal Detail:
Title:  Bioorganicheskaia khimiia     Volume:  37     ISSN:  0132-3423     ISO Abbreviation:  Bioorg. Khim.     Publication Date:    2011 Sep-Oct
Date Detail:
Created Date:  2012-02-15     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  7804941     Medline TA:  Bioorg Khim     Country:  Russia (Federation)    
Other Details:
Languages:  rus     Pagination:  616-26     Citation Subset:  IM    
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