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Expression of jumper ant (Myrmecia pilosula) venom allergens: Post‐translational processing of allergen gene products
Author(s) -
Donovan G. R.,
Street M. D.,
Tetaz T.,
Smith A. I.,
Alewood D.,
Alewood P.,
Sutherland S. K.,
Baldo B. A.
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201022
Subject(s) - venom , allergen , jumper , homologous chromosome , gene , ant , biology , myr , chemistry , microbiology and biotechnology , biochemistry , immunology , allergy , genome , ecology , computer science , operating system
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.