Publication no. C-2003-0211-06R |  VIEW ARTICLE

Identification of Disulfide Proteins in the Salt Soluble Fraction of Rice (Oryza sativa) Seed.

Hiroyuki Yano (1,2) and Shigeru Kuroda (1). (1) Department of Rice Research, National Agricultural Research Center, Inada 1-2-1 Joetsu, Niigata, Japan 943-0193. (2) Corresponding author. E-mail: <hyano@affrc.go.jp> Phone and Fax: +81-255263245. Cereal Chem. 80(2):172-174. Accepted November 18, 2002. Copyright 2003 American Association of Cereal Chemists, Inc.

Evidence has been accumulating to suggest that disulfide bonding is one of the key causes of allergenicity. Recently we developed the “disulfide proteome”, a technique for the comprehensive analysis of disulfide bonding of proteins. We applied this new technique to the rice seed’s salt-soluble fraction, which has long been known to be allergenic. Most proteins in the fraction, including alpha-amylase/trypsin inhibitor, alpha-globulin, and glutelin fragments, have formed intramolecular disulfide bonds. Also, unknown proteins, including one sharing similarities with known allergens, had disulfide bonds, from which we can infer possible allergenicity. This is a preliminary study to screen allergens from the basis of disulfide bonding.