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KMID : 0368420080510040297
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Journal of Plant Biology
2008 Volume.51 No. 4 p.297 ~ p.301
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The effect of DTT in protein preparations for proteomic analysis: Removal of a highly abundant plant enzyme, ribulose bisphosphate carboxylase/oxygenase
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Cho Jin-Hwan
Hwang Hee-Youn
Cho Man-Ho
Kwon Yong-Kook
Jeon Jong-Seong
Bhoo Seong-Hee
Hahn Tae-Ryong
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Abstract
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Rubisco is a major photosynthetic plant enzyme in the chloroplasts, catalyzing a photosynthetic reaction through carboxylation and oxygenation in the leaves. Despite its biological importance, its high abundance causes difficulties in the proper separation of protein mixtures during 2-dimensional gel electrophoresis (2-DE). Here, we resolved those plant soluble proteins by efficiently removing Rubisco. This resulted in a high quality and resolution of 2-DE gels. Rubisco removal was achieved through aggregation in the presence of a high DTT concentration, which subsequently increased the visualization of less abundant proteins and reduced horizontal streaking. This simple method may provide a means for finding more biologically important protein targets via plant proteomics.
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KEYWORD
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2-DE, abundant proteins, plant proteomics, protein solubilization, Rubisco
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