H. Tsuji et al., PURIFICATION AND CHARACTERIZATION OF SOYBEAN ALLERGEN GLY-M-BD 28K, Bioscience, biotechnology, and biochemistry, 61(6), 1997, pp. 942-947
At least 15 allergenic proteins have been found in soybean using the s
era of soybean-sensitive patients with atopic dermatitis [T. Ogawa et
al., J. Nutr. Sci. Vitaminol., 35, 555-565 (1991)], In the present stu
dy, a monoclonal antibody (mAb) against Gly m Ed 28K, one of the major
allergens of soybean, was prepared, and Gly m Ed 28K was purified fro
m defatted soybean flakes by five purification steps, including immuno
affinity chromatography with the mAb as a ligand. The purified allerge
n was found to be a glycoprotein with a molecular mass of 26 kDa, Duri
ng the purification process the allergen was converted to more acidic
proteins with the same molecular mass, suggesting that the allergen is
unstable, The sugar composition and amino acid sequence of Gly m Ed 2
8K suggest that the allergen is a new glycoprotein with an Asn-linked
sugar moiety, The distribution of the allergen in soybean products was
examined by an immunoblotting technique with the mAb.