日本プロテオーム学会大会要旨集
第2回ヒトプロテオーム学会
セッションID: 1S4-2
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リン酸化タンパク質検出法の比較
*大房 健山縣 彰吉里 勝利
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Protein phosphorylation is one of the most important post-translational modification of proteins and plays a variety of biological processes such as differentiation, cell division, metabolism, cell-cell communication, and disease. The phosphorylation of a protein cannot be predicted from its DNA sequence, and is determined only by analyzing protein itself. Proteome analysis using 2D gel electrophoresis is a most powerful technique for solving the composition of total proteins contained in cellular proteins. Although several separation techniques of proteins has been employed in proteome analyses, one of the most common technique is two-dimensional electrophoresis which simultaneously resolve several thousands of proteins including protein variants produced by the co- or post-translational processing such as phosphorylation, glycosylation, and degradation. We devised a new method (phosphoproteomics) to comprehensively map phosphoproteins on 2-D gels by comparing gel images of phosphatase-treated and non-treated samples.

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© 2004 日本プロテオーム学会(日本ヒトプロテオーム機構)
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