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dc.titleProfiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model
dc.contributor.authorRajaseger, G.
dc.contributor.authorLim, C.L.
dc.contributor.authorLee, K.W.
dc.contributor.authorArjunan, P.
dc.contributor.authorJia, L.
dc.contributor.authorMoochhala, S.
dc.identifier.citationRajaseger, G., Lim, C.L., Lee, K.W., Arjunan, P., Jia, L., Moochhala, S. (2006). Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model. Frontiers in Bioscience 11 (SUPPL. 3) : 2924-2928. ScholarBank@NUS Repository.
dc.description.abstractHeat induced complications cause an increase in a large number of proteins which play a role in diverse pathways during heat shock. A detailed characterization of these proteins is essential for understanding the molecular mechanisms involved in heat stroke. In this report, the proteins present in rat liver were compared at 37 °C (control) and at core temperature (Tc) 42 °C (heat stress) by 1D PAGE and MALDI/MS/MS. Among proteins identified in the sample after heat stress are dimethyglycine dehydrogenase, transketolase, carboxylic ester hydrolase, pyruvate kinase, L-type pyruvate kinase, arginosuccinate synthetase; fumarylacetoacetate hydrolase and peptidylpropyl isomerase A. These findings show that analysis of large scale proteins by MALDI/MS/MS provides a better understanding of the molecular mechanisms associated with heat shock. The resolution of proteins examined by 1D-PAGE was less than that obtained with 2D-PAGE. More specifically, 2D-PAGE allows better identification of low molecular weight proteins that can not be resolved by 1D-PAGE.
dc.subject1D PAGE
dc.subjectHeat stress
dc.subjectHepatocellular proteins
dc.subjectPolyacrylamide gel electrophoresis
dc.subjectRat model
dc.description.sourcetitleFrontiers in Bioscience
dc.description.issueSUPPL. 3
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