Expression of jumper ant (Myrmecia pilosula) venom allergens: Post‐translational processing of allergen gene products
1996
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.
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