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Affinity‐based proteomic profiling: Problems and achievements
Author(s) -
Medvedev Alexei,
Kopylov Arthur,
Buneeva Olga,
Zgoda Victor,
Archakov Alexander
Publication year - 2012
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.201100373
Subject(s) - affinity chromatography , proteomics , chemistry , computational biology , glycoprotein , biochemistry , proteome , fractionation , profiling (computer programming) , biology , chromatography , enzyme , gene , computer science , operating system
Affinity chromatography becomes a more and more popular method used in proteomic studies for separation of various groups of proteins (subproteomes). The review highlights the role of affinity chromatography fractionation for proteomic profiling of the most of intensively studied groups of proteins including cyclic nucleotide‐binding proteins, protein kinases (kinomes), phosphoproteins, glycoproteins, ubiquitinated proteins. Special attention is paid to the use of affinity chromatography for the characterization of small‐molecule protein targets. The latter is especially important for the elucidation of direct protein targets of potential drug substances for evaluation of their possible side‐effects or additional pharmacological application.