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Titlebook: Handbook of Proteomic Methods; P. Michael Conn Book 2003 Springer Science+Business Media New York 2003 Amino acid.Proteomics.proteins.tran

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书目名称Handbook of Proteomic Methods
编辑P. Michael Conn
视频video
概述Includes supplementary material:
图书封面Titlebook: Handbook of Proteomic Methods;  P. Michael Conn Book 2003 Springer Science+Business Media New York 2003 Amino acid.Proteomics.proteins.tran
描述A compendium of thirty-four powerful techniques for identifying and analyzing the diversity of proteins expressed in cells. Thee readily reproducible proteomic methods range from general to specific techniques, and include methods for data analysis, posttranslational modification, and its variants and isoforms. Additional methods demonstrate the application of proteomics to the discovery of serological tumor markers, to identifying the determinants of sensitivity to antitumor drugs, and to specialized fields, such as endocrinology, plant biology, nephrology, and urology.
出版日期Book 2003
关键词Amino acid; Proteomics; proteins; transcription; translation
版次1
doihttps://doi.org/10.1007/978-1-59259-414-6
isbn_softcover978-1-61737-504-0
isbn_ebook978-1-59259-414-6
copyrightSpringer Science+Business Media New York 2003
The information of publication is updating

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Selective Chemical Cleavage Methods in Proteomics, Including C-Terminal Successive Degradationng a cleavage type other than conventional HC1 hydrolysis. Partial acid hydrolysis using high concentrations of perflooric acid have indicated a novel cleavage specificity of peptide bonds, different from those of either Sanger’s high-concentration acid hydrolysis . or the conventional dilute-acid h
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A Combined Radiolabeling and Silver Staining Technique for Improved Visualization and Localization o (MS) is rapidly becoming the key tool for protein identification. When combined, 2-DGE and MS form the current operating paradigm for classical proteomics. One of the key challenges of proteome research is that of detecting and identifying all the elements (proteins) of a proteome. Silver staining
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Di- and Tri-Chromatic Fluorescence Detection on Western Blotsun replicate gels, using one for general protein staining and the other for immunoblotting. Similar procedures are often employed to visualize total protein and glycoprotein profiles by lectin blotting. However, the multiple manipulations required for electrophoresis and blotting often result in an
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Stable Isotope Labeling with Amino Acids as an Aid to Protein Identification in Peptide Mass Fingerppots on one-dimensional (1-D) or two-dimensional (2-D) gels, as single proteins or mixtures isolated by chromatographic steps, or by affinity purification. In all instances, the protein to be identified is first isolated and then digested with a protease of defined specificity, such as trypsin or en
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