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020 _a9781592591817
024 7 _a10.1385/1592591817
_2doi
040 _aES-MaUEC
_bspa
_cES-MaUEC
_dES-MaUEC
050 4 _aQH450
_b2002 EB
245 0 0 _aPosttranslational Modification of Proteins :
_bTools for Functional Proteomics
_cedited by Christoph Kannicht
250 _a1st edition 2002
264 1 _aTotowa, NJ
_bHumana Press
_c2002
300 _a1 recurso en línea (XI, 322 páginas)
_b19 ilustraciones
336 _atexto
_btxt
_2rdacontent
337 _aelectrónico
_bc
_2rdamedia
338 _arecurso electrónico
_bcr
_2rdacarrier
347 _aarchivo de texto
_bPDF
490 0 _aMethods in Molecular Biology
_x1940-6029
_v194
505 0 _aAssignment 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.
520 _aThe 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.
988 _aSpringer_Protocols_2002
650 7 _2embne
_9162770
_aExpresión génica
776 0 8 _iPrinted edition:
_z9781489938640
776 0 8 _iPrinted edition:
_z9780896036789
776 0 8 _iPrinted edition:
_z9781489938633
856 4 0 _uhttps://go.openathens.net/redirector/universidadeuropea.es?url=https://doi.org/10.1385/1592591817
_zAcceso a este recurso digital (usuarios Universidad Europea de Madrid)
942 _2lcc
_cLE
998 _b12/2023
_dz
_eb
_zSI