
<ArticleTitle>Isolation and partial characterization of a 46-kd allergen of Bermuda grass pollen.</ArticleTitle>
<AbstractText><prot>Cyn d Bd46K</prot>, a 46-kD component of Bermuda grass (Cynodon dactylon) pollen, had been identified as an allergenic constituent. In the present study two-dimensional (2D) gel electrophoresis illustrated the presence of five acidic isoforms in <prot>Cyn d Bd46K</prot>, and this molecule was purified by monoclonal antibody (MAb) affinity chromatography for further characterization. Using a digoxigenin-labeled lectin-binding assay, the elucidating protein was disclosed to be a glycoprotein with terminal mannose. The involvement of a carbohydrate moiety in the allergenicity and antigenicity of the elucidated molecule was demonstrated with sodium-periodate-treated <prot>Cyn d Bd46K</prot>, which reduced binding to its specific MAb and human IgE. We were unable to identify the N-terminal amino acid sequences of <prot>Cyn d Bd46K</prot>, but some internal amino acid sequences were disclosed by microsequencing some fragments cleaved by Achromobacter protease I and fractionated by reversed-phase column chromatography. The amino acid sequences of 4 identified <prot>Cyn d Bd46K</prot> internal peptide fragments were found to be 25-71% identical with that of <prot>cytochrome c oxidase III</prot> from corn grass pollen. The present study provided important information for future experiments on the molecular cloning of the elucidated allergen.</AbstractText>
