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Çѱ¹½Ä¹°ÇÐȸ / v.51, no.4, 2008³â, pp.297-301
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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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| 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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| 2-DE;abundant proteins;plant proteomics;protein solubilization;Rubisco; |
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Journal of Plant Biology / v.51, no.4, 2008³â, pp.297-301
Çѱ¹½Ä¹°ÇÐȸ
ISSN : 1226-9239
UCI : G100:I100-KOI(KISTI1.1003/JNL.JAKO200828837395241)
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| ³í¹® Á¦°ø : KISTI Çѱ¹°úÇбâ¼úÁ¤º¸¿¬±¸¿ø |
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