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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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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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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.

116, 5513–5514. 8. , and Fukuda, T. (1994) Production of human PTH (1-34) via a recombinant DNA technique. Biochem. Biophys. Res. Commun. 200, 1735–1741. 9. Wu, J. and Watson, J. T. (1998) Optimization of the cleavage reaction for cyanylated cysteinyl proteins for efficient and simplified mass mapping. Anal. Biochem. 258, 268–276. 10. , Gage, D. , and Watson, J. T. (1996). A strategy to locate cysteine residues in proteins by specific chemical cleavage followed by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry.

T. (1997) A novel methodology for assignment of disulfide bond pairings in proteins. Protein Sci. 6, 391–398. 12. , and Watson, J. T. (1998) Disulfide mass mapping in proteins containing adjacent cysteines is possible with cyanylation/cleavage methodology. J. Am. Chem. Soc. 120, 5834–5835. 13. , Aposhian, H. , 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).

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