Abstract
This chapter discusses the methodology that has been used to obtain partial or complete purification of bacterial peptide chemoattractants, including the chemoattractant fMet-Leu-Phe (fMLP) from E. coli culture filtrates. For the latter, definitive demonstration of the formylmethionyl group has been obtained following high-pressure liquid chromatography (HPLC), using dipeptidyl carboxypeptidase/gas chromatography-mass spectroscopy (DCP/GC-MS) to determine the amino acid sequences. The simultaneous analysis of both biological and antigenic activities in the bacterial culture filtrates are invaluable steps in the purification of the chemotactic factors, especially the formylmethionyl peptides. Because multiple and structurally diverse biological substances are known to act as chemotactic factors for leukocytes, analysis of antigenic activity quickly allows the establishment of the class of chemoattractant. Thus, substantial biological activity may be detected in spite of a negative regulatory impact analysis (RIA). This same hypothesis would explain the inability to detect any formylmethionyl peptides by DCP/GC-MS. It is also possible that these activities are associated with peptides structurally unrelated to the formyl peptides.
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