Download e-book for kindle: Posttranslational Modifications of Proteins: Tools for by Christoph Kannicht (Ed.)
By Christoph Kannicht (Ed.)
Christoph Kannicht and a panel of hugely skilled researchers describe without difficulty reproducible equipment for detecting and examining the posttranslational alterations of protein, quite in regards to protein functionality, proteome study, and the characterization of pharmaceutical proteins. one of the equipment provided are these for reading 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 thoughts facilitate the research of glycosylphosphatidylinositols, lipid ameliorations, 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)
Neat trifluoroacetic acid (TFA). 2. 1% (w/v) Aqueous sodium acetate solution. 3. 15. National Scientific, BC16NA-BP) (see Note 4). 4. 4% (w/v) Sodium acetate (trihydrate)-2% (w/v) boric acid (granular) in methanol (see Note 3). 5. Anthranilic acid (AA) solution: Weigh approx 45 mg of anthranilic acid (2-amino benzoic acid) into a polypropylene vial. Add approx 30 mg of sodium cyanoborohydride. 5 mL of the sodium acetate-boric acidmethanol solution. (Note: Sodium cyanoborohydride is a poison and tends to absorb moisture readily from the air, which may affect the derivatization reaction.
5. Anumula, K. R. (1994) Quantitative determination of monosaccharides in glycoproteins by high performance liquid chromatography with highly sensitive fluorescence detection. Anal. Biochem. 220, 275–283. 6. Anumula, K. R. (1995) Novel fluorescent methods for quantitative determination of monosaccharides and sialic acids in glycoproteins by reversed phase high performance liquid chromatography, in Methods in Protein Structure Analysis (Atassi, M. Z. ), Plenum Press, New York, pp. 195–206. 7. Anumula, K.
2. Calculate the quantity of sialic acid (in pmol) per mg of protein taking into account dilution factors, sample volumes, and injection volumes used. 3. The moles of sialic acid per mole of protein is determined by the following formula: (pmol/mg of protein × MW) moles of sialic acid per mole of protein = ——–————————— 109 34 Saddic et al. where: 109 is the conversion factor from pmol to moles MW is the molecular weight of the protein as determined from the amino acid sequence. 5. 0% as determined by peak area.
Posttranslational Modifications of Proteins: Tools for Functional Proteomics (Methods in Molecular Biology Vol 194) by Christoph Kannicht (Ed.)