By Catherine Cooper
A set of vintage and state-of-the-art recommendations of excessive software in answering particular organic questions about amino acids. universal equipment comprise these in keeping with HPLC or fuel chromatography separation and research after precolumn derivatization. New ideas in response to capillary electrophoresis separation, high-performance anion alternate chromatography, and mass spectrometry also are provided. every one process is defined in step by step element to make sure profitable experimental effects and emphasizes pattern education, really the gathering and garage of physically fluids. up to date and hugely useful, Amino Acid research Protocols bargains analytical and scientific chemists, in addition to a huge diversity of organic and biomedical investigators, a wealthy compendium of laboratory instruments for the efficient research of either universal and unusual amino acids.
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Additional resources for Amino acids analysis Protocols
8. Silica-based C8 columns from different commercial sources produce base-line resolution of the 19 amino acid derivatives; nevertheless, the gradient slope of solvent B should be optimized for each column. S-Carboxymethyl-L-cysteine and tryptophan, if included, are also separated in a single chromatographic run (see ref. 2). 9. The identity of each peak is established by adding a threefold molar excess of the amino acid in question. A reagent blank should be run with each batch of the Marfey’s reagent to identify reagent-related peaks.
When samples containing a high concentration of protein or peptide are available in reasonable volume, there is no need to purify the sample further, simply dilute the sample with HPLC-grade water to a salt concentration that will not interfere with the analysis. 9. Acetonitrile (ACN) concentrations greater than 15% interfere with sample binding to PVDF. 1% TFA to reduce the concentration of ACN to less than 15%, prior to using the ProSorb cartidge. 10. Often proteins submitted for amino acid analysis contain detergents used in their preparation.
22. Molony, M. , Mulkerrin, M. , and Harris, R. J. (1998) Hydroxylation of Lys residues reduces their susceptibility to digestion by trypsin and lysyl endopeptidase. Anal. Biochem. 258, 136–137. 23. Harris, R. J. and Spellman, M. W. (1993) O-Linked fucose and other post-translational modifications unique to EGF modules. Glycobiol. 3, 219–224 24. Yan, S. , Chao, Y. , and van Halbeek, H. (1993) Novel Asn-linked oligosaccharides terminating in GalNAcβ(1→4)[Fucα(1→3)]GlcNAcβ(1→•) are present in recombinant human Protein C expressed in human kidney 293 cells.
Amino acids analysis Protocols by Catherine Cooper