Abstract
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.
MeSH terms
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Alkylation
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Allergens*
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Amino Acid Sequence
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Animals
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Ant Venoms / chemistry*
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Ant Venoms / genetics*
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Ant Venoms / immunology
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Ants / genetics*
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DNA, Complementary / immunology
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Disulfides / chemistry
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Electrophoresis, Polyacrylamide Gel / methods
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Immunoblotting
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Insect Proteins*
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Molecular Sequence Data
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Molecular Weight
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Oxidation-Reduction
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Protein Precursors / genetics
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Protein Precursors / metabolism
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Protein Processing, Post-Translational*
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Sequence Homology, Amino Acid
Substances
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Allergens
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Ant Venoms
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DNA, Complementary
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Disulfides
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Insect Proteins
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Myr p I
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Myr p II protein, Myrmecia pilosula
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Protein Precursors