title: N-terminal amino acid sequence homologies of group V grass pollen allergens.
abstract: In an earlier study, we presented data regarding the immunoaffinity purification and N-terminal sequencing of a major pollen allergen from orchard/cocks-foot grass (Dactylis glomerata), now identified as the group V allergen Dac g V. In this paper, we have extended our investigations to include group V allergens from other grass species. Our data confirm the presence of group V-restricted characteristic N-terminal amino acid sequences containing a high alanine and hydroxyproline (P') rather than proline (P) content, and based upon two conserved elements (ADAGY and TPA/TP'A).
authors.affiliation: University Department of Clinical Chemistry, Wolfson Research Laboratories, Queen Elizabeth Medical Centre, Edgbaston, Birmingham, UK.
authors.forename: A M
authors.initials: AM
authors.lastname: Roberts
authors.forename: R
authors.initials: R
authors.lastname: van Ree
authors.forename: J
authors.initials: J
authors.lastname: Emly
authors.forename: S M
authors.initials: SM
authors.lastname: Cardy
authors.forename: M M
authors.initials: MM
authors.lastname: Rottier
authors.forename: M R
authors.initials: MR
authors.lastname: Walker
mesh_terms: D000485:Allergens / Q000737:chemistry*; D000595:Amino Acid Sequence; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry / Q000276:immunology*; D006109:Poaceae / Q000737:chemistry / Q000276:immunology*; D011058:Pollen / Q000737:chemistry* / Q000276:immunology; D016415:Sequence Alignment
chemical_list: D000485:Allergens; D010940:Plant Proteins