The isolation and partial characterization of neutrophil chemotactic factors from Escherichia coli.
Heat-stable, chemotactically active peptides have been obtained from Escherichia coli culture filtrates. They range in size between 150 and 1500 daltons and are anionic at neutral pH. Free carboxyl groups but not free amino groups appear to be required for activity. The N-terminal group may be blocked. There do not appear to be internal aromatic or basic residues in the chemotactically active fractions. A highly purified, not completely characterized, fraction was found to contain aspartic acid, serine, glutamic acid, alanine, and glycine.
D000107:Acetylation; D000409:Alanine / Q000032:analysis; D000818:Animals; D001202:Ascitic Fluid / Q000166:cytology; D001224:Aspartic Acid / Q000032:analysis; D001426:Bacterial Proteins / Q000032:analysis; D001431:Bacteriological Techniques; D002633:Chemotaxis; D002850:Chromatography, Gel; D002855:Chromatography, Thin Layer; D003182:Complement C5; D003619:Dansyl Compounds; D004591:Electrophoresis, Polyacrylamide Gel; D004798:Enzymes; D004926:Escherichia coli / Q000276:immunology*; D005971:Glutamates / Q000032:analysis; D005998:Glycine / Q000032:analysis; D009504:Neutrophils / Q000276:immunology*; D010455:Peptides / Q000302:isolation & purification*; D010504:Periodic Acid; D011817:Rabbits; D012694:Serine / Q000032:analysis
D001426:Bacterial Proteins; D003182:Complement C5; D003619:Dansyl Compounds; D004798:Enzymes; D005971:Glutamates; D010455:Peptides; D010504:Periodic Acid; D001224:Aspartic Acid; D012694:Serine; D000409:Alanine; D005998:Glycine