Enhanced proteome profiling by inhibiting proteolysis with small heat shock proteins

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Proteolytic degradation is one of the critical problems in two-dimensional electrophoresis (2-DE). Here we report that small heat shock proteins (sHsps), including IbpA(Ec) and IbpB(Ec) from Escherichia coli and Hsp26(Sc) from Saccharomyces cerevisiae, are able to protect proteins in vitro from proteolytic degradation. Addition of sHsps during 2-DE of human serum or whole cell extracts of E. coli, Mannheimia succinciproducens, Arabidopsis thaliana, and human kidney cells allowed detection of up to 50% more protein spots than those obtainable with currently available protease inhibitors. Therefore, the use of sHsps during 2-DE significantly improves proteome profiling by generally enabling the detection of many more protein spots that could not be seen previously.
Publisher
AMER CHEMICAL SOC
Issue Date
2005-11
Language
English
Article Type
Article
Keywords

2-DIMENSIONAL GEL-ELECTROPHORESIS; ESCHERICHIA-COLI; PLANT-TISSUES; EXPRESSION; IBPB

Citation

JOURNAL OF PROTEOME RESEARCH, v.4, pp.2429 - 2434

ISSN
1535-3893
DOI
10.1021/pr050259m
URI
http://hdl.handle.net/10203/21227
Appears in Collection
CBE-Journal Papers(저널논문)
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