N-terminal amino acid sequence homologies of group V grass pollen allergens.
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).
Roberts
A M
AM
University Department of Clinical Chemistry, Wolfson Research Laboratories, Queen Elizabeth Medical Centre, Edgbaston, Birmingham, UK.
van Ree
R
R
Emly
J
J
Cardy
S M
SM
Rottier
M M
MM
Walker
M R
MR
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
D000485:Allergens; D010940:Plant Proteins