1996/08/01 by Gregory R. Donovan, Michael Street, T. Tetaz +5 · 7 citations
Medicine · Agricultural and Biological Sciences · Chemistry · #Allergic Rhinitis and Sensitization #Food Allergy and Anaphylaxis Research #Insect and Pesticide Research #Venom #Allergen #Jumper #Homologous chromosome #Gene #ANT #Biology #myr #Chemistry #Molecular biology #Biochemistry #Immunology #Allergy #Genome
paper · doi:10.1080/15216549600201022
openalex publication_date 1996/08/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/05/21
N-terminal analyses of electrophoretically-separated allergenic polypeptides of the venom of the jumper ant M. pilosula showed that five out of the six allergenic polypeptides identified are homologous with the cloned major allergen Myr p I and may be derived from a single precursor polypeptide. The sixth polypeptide is homologous with a second cloned major allergen, Myr p II which is expressed as a single precursor polypeptide but exists in its native form as a disulphide bond-linked complex.