PURIFICATION AND CHARACTERIZATION OF SOYBEAN ALLERGEN GLY-M-BD 28K

Citation
H. Tsuji et al., PURIFICATION AND CHARACTERIZATION OF SOYBEAN ALLERGEN GLY-M-BD 28K, Bioscience, biotechnology, and biochemistry, 61(6), 1997, pp. 942-947
Citations number
21
Categorie Soggetti
Biology,Agriculture,"Biothechnology & Applied Migrobiology","Food Science & Tenology
ISSN journal
09168451
Volume
61
Issue
6
Year of publication
1997
Pages
942 - 947
Database
ISI
SICI code
0916-8451(1997)61:6<942:PACOSA>2.0.ZU;2-5
Abstract
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.