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N-terminal amino acid sequence homologies of group V grass pollen allergens
A M Roberts1, R van Ree, J Emly
1University Department of Clinical Chemistry, Wolfson Research Laboratories, Queen Elizabeth Medical Centre, Edgbaston, Birmingham, UK.
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).