By Christoph Kannicht (Ed.)
Christoph Kannicht and a panel of hugely skilled researchers describe with no trouble reproducible tools for detecting and examining the posttranslational alterations of protein, really with reference to protein functionality, proteome examine, and the characterization of pharmaceutical proteins. one of the equipment provided are these for studying the project of disulfide bond websites in proteins, protein N-glycosylation and protein O-glycosylation, and oligosaccharides current at particular unmarried glycosylation websites in a protein. extra robust innovations facilitate the research of glycosylphosphatidylinositols, lipid alterations, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation.
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Extra info for Posttranslational Modifications of Proteins: Tools for Functional Proteomics (Methods in Molecular Biology Vol 194)
Example text
Therefore, if possible, all steps during the purification procedure should be performed at daylight and the labeled oligosaccharides are stored at –20°C in the dark. References 1. , and Parekh, R. (1993) Use of Hydrazine to release an intact and unreduced form both from N- and O-linked oligosaccharides from glycoproteins. Biochemistry 32, 679–693. 2. Patel, T. P. and Parekh, R. B. (1994) Release of oligosaccharides from glycoproteins by hydrazinolysis. Methods Enzymol. 230, 57–66. 3. , (1982) Hydrazinolysis of asparaginelinked sugar chains to produce free oligosaccharides.
Carbohydrate composition analysis of glycoproteins is similar to amino acid analysis of proteins. Just as an accurate amino acid composition is critical to protein-structure determination and identification by database searching, the accurate determination of the carbohydrate composition of a glycoprotein provides information as to the type and extent of glycosylation. In order From: Posttranslational Modifications of Proteins: Tools for Functional Proteomics Edited by: C. , Totowa, NJ 23 24 Saddic et al.
1984) Rabbit muscle creatine phosphokinase cDNA clone, primary structure and detection of human homologues. J. Biol. Chem. 259, 14,317–14,320. 22 Wu and Watson 14. Gray, W. R. (1993). Disulfide structures of highly bridged peptides: a new strategy for analysis. Protein Sci. 2, 1732–1748. 15. Gray, W. R. (1993) Echistatin disulfide bridges: selective reduction and linkage assignment. Protein Sci. 2, 1749–1755. 16. Schutte, C. , Glombitza, G. , and Sandhoff, K. (1998) Complete localization of disulfide bonds in GM2 activator protein.