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|Title:||Profiling of hepatocellular proteins by 1D PAGE-MALDI/MS/MS in a rat heat stress model|
Polyacrylamide gel electrophoresis
|Citation:||Rajaseger, 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. https://doi.org/10.2741/2021|
|Abstract:||Heat 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.|
|Source Title:||Frontiers in Bioscience|
|Appears in Collections:||Staff Publications|
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