Isolation and partial characterization of Bermuda grass pollen allergen, BG-60a
Article first published online: 27 APR 2006
Clinical & Experimental Allergy
Volume 21, Issue 4, pages 449–455, July 1991
How to Cite
SU, S. N., LAU, G. X., TSAI, J. J., YANG, S. Y., SHEN, H. D. and HAN, S. H. (1991), Isolation and partial characterization of Bermuda grass pollen allergen, BG-60a. Clinical & Experimental Allergy, 21: 449–455. doi: 10.1111/j.1365-2222.1991.tb01685.x
- Issue published online: 27 APR 2006
- Article first published online: 27 APR 2006
- Revised 31 August 1989; revised 3 January 1991; accepted 15 January 1991.
In an earlier study we showed that Bermuda grass (Cynodon dactylon) pollen contains at least 12 IgE-binding proteins that can be analysed by immunoblot technique. One of the active components (BG-60) proved to be a basic protein of glycoprotein nature. It contained about 28% carbohydrate as determined from the dry weight and consisted of four molecules. One of the components was purified from the pollen extract by a combination of ammonium sulphate precipitation, ion-exchange chromatography on carboxymethyl-TSK, gel filtration on Ultrogel AcA 44 and chromatofocusing. Its molecular weight was approximately 60 kD by SDS PAGE and 34 kD by gel filtration chromalography. The isoelectric point of the antigen was about 9.7. The homogeneity of the antigen BG-60a was assessed by one single are of immunoprecipitation both in immanodiffusion and crossed immunoelectrophoresis and by one single band after SDS-PAGE. Its allergenicity was demonstrated by direct intradermal skin test on allergic patients and by examining IgE-binding reactivity with allergic patients' serum.