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Extra resources for Amino Acid Analysis Protocols (Methods in Molecular Biology Vol 159)
16. Lundell, N. and Schreitmüller, T. (1999) Sample preparation for peptide mapping — a pharmaceutical quality-control perspective. Anal. Biochem. 266, 31–47. 17. Jones, M. , Merewether, L. , Clogston, C. , and Lu, H. S. (1994) Peptide map analysis of recombinant human granulocyte stimulating factor: elimination of methionine modification and nonspecific cleavages. Anal. Biochem. 216, 135–146. 18. Allen, G. (1989) Determination of the carboxy-terminal residue, in Sequencing of Proteins and Peptides, Elsevier, Amsterdam and New York, pp.
Instrument Settings 1. Set the column heater to 38°C. 2. Set the fluorescence-detector excitation wavelength at 248 nm and the emission wavelength at 395 nm. Precolumn Derivatization with AQC 43 Fig. 1. Typical separation for a hydrolysate standard. The injected volume was 5 µL with a total of 50 pmol of each amino acid (25 pmol cystine) injected. Detection was accomplished by fluorescence with excitation at 248 nm and emission at 395 nm. The chromatographic conditions were those described in the methods section.
Pyridylethylcysteine (PECys) is very basic, and elutes after Arg (Fig. 8). 27. When monitoring Cys alkylation conditions, attention should be paid to methionine recoveries, as the conditions (such as trace metals or residual O2) that affect Met recoveries will also affect CMCys recoveries. In addition, methionine sulfoxide can coelute with CMCys; therefore, samples should be analyzed promptly after acid removal. References 1. Moore, S. and Stein, W. H. (1958) Chromatographic determination of amino acids by the use of automatic recording equipment.