By Christopher Walsh
Christoph Kannicht and a panel of hugely skilled researchers describe with ease reproducible equipment for detecting and reading the posttranslational ameliorations of protein, fairly with reference to protein functionality, proteome learn, and the characterization of pharmaceutical proteins. one of the tools provided are these for examining the task 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 strong strategies facilitate the research of glycosylphosphatidylinositols, lipid transformations, protein phosphorylation and sulfation, protein methylation and acetylation, a-amidation, g-glutamate, isoaspartate, and lysine hydroxylation.
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Additional info for Posttranslational modification of proteins
The derivative is separated from excess reagent by RP-HPLC for quantitation using fluorescence detection (6,7). The resulting peak areas are compared to those of concomitantly derivatized sialic acid standards to determine the amount of the sialic acids (N-acetyl and N-glycolylneuraminic acids). The methods described here are based on the use of highly fluorescent tags. They offer the most sensitive approach to analyze glycoproteins at this time, and therefore, these methods are suitable for analyzing samples available in limited amounts.
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