By Cooper C., Packer N.
Proteome platforms Ltd, North Ryde, Australia. Describes various amino acid research concepts and the way each one process can be utilized to reply to particular biologic questions.
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Extra info for Amino Acid Analysis Protocols (Methods in Molecular Biology Vol 159)
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.
19. In the standard amino acid analysis method (Table 1), Hyl coelutes with histidine, so it would not be observed in an intact protein that contains His, and it might be misinterpreted in a peptide fraction. The long delay for the second buffer change is needed to increase the resolution of Hyl from ammonia. Hyl appears as a partially resolved doublet peak due to racemization of the δ carbon during hydrolysis; therefore, the peak areas are summed. 20. Once it has been determined that Hyl is present, peptide maps may be used to assign the site provided the investigator is aware that Hyl–Gly bonds are fairly resistant to trypsin and endoproteinase Lys-C digestion (22).
Other HPLC systems can be used. To use a high-pressure binary gradient, use the alternate Eluent B. A typical gradient is shown in Table 2. Use a total run-time of 50 min to equilibrate the column 12. 0). One potential source is nonvolatile acid formation during the hydrolysis. Phosphate salt or sodium dodecyl sulfate will be converted to their respective acids, and will not be removed by vacuum drying. If excess acid is present, it may be neutralized with a TEA/ethanol/water solution (2:2:1, v/v).