title: Identification of formyl Met-Leu-Phe in culture filtrates of Helicobacter pylori.
abstract: Helicobacter pylori synthesizes and secretes a substance which co-chromatographs and is antigenically cross-reactive with the bacterial chemotactic peptide fMet-Leu-Phe. Using reverse phase and affinity chromatography this substance has now been purified. Carboxypeptidase Y microsequencing has verified that this material is fMet-Leu-Phe. The infiltration of polymorphonuclear leucocytes to sites of H. pylori infection may be a response to mucosal permeation of soluble, diffusable bioreactive substances such as fMet-Leu-Phe.
authors: Department of Experimental Medicine, Wellcome Medical Research Institute, University of Otago Medical School, Dunedin, New Zealand.
authors: M F
authors: MF
authors: Broom
authors: R M
authors: RM
authors: Sherriff
authors: D
authors: D
authors: Munster
authors: V S
authors: VS
authors: Chadwick
mesh_terms: D000595:Amino Acid Sequence; D002268:Carboxypeptidases; D002846:Chromatography, Affinity; D003470:Culture Media; D016480:Helicobacter pylori / Q000737:chemistry* / Q000378:metabolism; D008969:Molecular Sequence Data; D009240:N-Formylmethionine Leucyl-Phenylalanine / Q000302:isolation & purification* / Q000378:metabolism; D011863:Radioimmunoassay
chemical_list: D003470:Culture Media; D009240:N-Formylmethionine Leucyl-Phenylalanine; D002268:Carboxypeptidases; C022633:serine carboxypeptidase