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Posttranslational Modifications of Proteins : Tools for Functional Proteomics / edited by Christoph Kannicht.

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Holman Biotech Commons QH506 .M45 v.1 (1984)-v.20 (1993),v.22 (1994),v.24 (1994)-v.53 (1996), v.42 (1995) and v.51 (1995) reported missing 3-13-2000 v.55 (1995),v.58 (1996)-v.63 (1997), v.65 (1996)-v.154 (2001), v.156 (2001)-190 (2002), v.192 (2002)-v.407 (2007) v.409 (2007)-v.416 (2008),v.418 (2008)-v.466 v.468-v.490,v.492,v.494,v.496-499 501-506,508,510-512,514,516-517,519-536 538,540-569,571 573-589,591-608,610-615,617,620-627,630-633,636,638,642
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Format:
Book
Contributor:
Kannicht, Christoph, editor.
SpringerLink (Online service)
Series:
Methods in molecular biology 1064-3745 ; 194.
Springer Protocols (Springer-12345)
Methods in Molecular Biology™, 1064-3745 ; 194
Language:
English
Subjects (All):
Life sciences.
Cytology.
Life Sciences.
Cell Biology.
Local Subjects:
Life Sciences.
Cell Biology.
Physical Description:
1 online resource (XI, 322 pages) : 19 illustrations.
Contained In:
Springer eBooks
Place of Publication:
Totowa, NJ : Humana Press, 2002.
System Details:
text file PDF
Summary:
The majority of all proteins undergo posttranslational modifications that significantly alter their physical and chemical properties, including their folding and conformation distribution, their stability, and, consequently, their activity and function. In Posttranslational Modifications of Proteins: Tools for Functional Proteomics, Christoph Kannicht and a panel of highly experienced researchers describe readily reproducible methods for detecting and analyzing the most important of these modifications, particularly with regard to protein function, proteome research, and the characterization of pharmaceutical proteins. Among the methods presented are those for analyzing the assignment of disulfide bond sites in proteins, protein N-glycosylation and protein O-glycosylation, and oligosaccharides present at specific single glycosylation sites in a protein. Additional powerful techniques facilitate the analysis of glycosylphosphatidylinositols, lipid modifications, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation. Comprehensive and state-of-the-art, Posttranslational Modifications of Proteins: Tools for Functional Proteomics serves as a highly practical guide for all investigators of protein structure-function relationships not only in chemical and pharmaceutical research, but also throughout the rapidly growing field of functional proteomics.
Contents:
Assignment of Disulfide Bonds in Proteins by Chemical Cleavage and Peptide Mapping by Mass Spectrometry
Carbohydrate Composition Analysis of Glycoproteins Using Highly Sensitive Fluorescence Detection Methods
Enzymatical Hydrolysis of N-Glycans from Glycoproteins and Fluorescent Labeling by 2-Aminobenzamide (2-AB)
Separation of N-Glycans by HPLC
Enzymatic Sequence Analysis of N-Glycans
Immunological Detection of O-GlcNAc
Analysis of O-Glycosylation
Characterization of Site-Specific Glycosylation
Monitoring Glycosylation of Therapeutic Glycoproteins for Consistency Using Highly Fluorescent Anthranilic Acid
Metabolic Labeling and Structural Analysis of Glycosylphosphatidylinositols from Parasitic Protozoa
Analysis of S-Acylation of Proteins
Immunoblotting Methods for the Study of Protein Ubiquitination
Analysis of Methylation and Acetylation in E. coli Ribosomal Proteins
Identification of In Vivo Protein Phosphorylation Sites with Mass Spectrometry
Analysis of Tyrosine-O-Sulfation
?-Amidated Peptides: Approaches for Analysis
?-Glutamate and p-Hydroxyaspartate in Proteins
Detection of isoAspartate Residues as a Posttranslational Modification of Proteins and Peptides
Lysine Hydroxylation and Crosslinking of Collagen
Heterologous Expression in Endocrine Cells for Analysis of Posttranslational Modifications
2D-Electrophoresis: Detection of Glycosylation and Influence on Spot Pattern.
Other Format:
Printed edition:
ISBN:
9781592591817
Access Restriction:
Restricted for use by site license.

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