[Isolation and partial characterization of allergen from Bermuda grass pollen]

Allergens of bermuda grass pollen extract have been studied and identified. Immunoblotting studies revealed that at least 12 SDS-denatured polypeptide showed IgE-binding activity. Molecular weight was estimated between 10,000 to 90,000 daltons. An allergenic component was isolated by a combination of ion exchange chromatography and gel filtration chromatography. The allergen preparation was shown to be homogeneous by PAGE and SDS-PAGE studies. Allergen was found to be an acidic protein with a molecular size of the order of 16,300 daltons. Ultraviolet spectrum scanning showed weak absorption at 280 nm. Amino acid analysis revealed that the purified allergen contained no tyrosine, proline and cysteine residues but contained a high percentage of glutamic acid and aspartic acid residues. The results of amino analysis indicate that tyrosine, proline and cysteine residues are not involved in the allergenic determinant site.