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- W2073851452 abstract "The pollen of Ricinus communis L., a potentially allergenic plant, was extracted to identify the allergenic determinants responsible for causing respiratory disorders. The soluble proteins were extracted and subjected to ammonium sulphate precipitation at 80% saturation and the total protein separated on 12% SDS-Polyacrylamide gel. In order to avoid the time consuming and expensive biochemical methods of column chromatography, each band was directly recovered from the gel by electroelution and the allergenic proteins identified directly by skin tests, without the necessity of Phadezym RAST or ELISA inhibition by reaction with serum IgE, the general procedure to identify the allergens. The fourth and the fifth band in the protein profile of R. communis pollen, RC4 (77 kD) and RC5 (66 kD) were the two major allergenic components. RC3 (91 kD) also induced a considerable amount of reactivity in sensitive patients. Contrary to the earlier reports of protein bands of R. communis ranging from 14 kD to 70 kD, 4 b..." @default.
- W2073851452 created "2016-06-24" @default.
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- W2073851452 date "1999-10-01" @default.
- W2073851452 modified "2023-09-26" @default.
- W2073851452 title "Identification and partial characterization of the allergenic proteins ofRicinus communisL. pollen - a new approach" @default.
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- W2073851452 doi "https://doi.org/10.1080/001731300750044546" @default.
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