Proteins are essential to the seed development and quality formation of buckwheat．Single seeds of common buckwheat cultivar Suwon No．1 when subjected to SDS-PAGE revealed very high polymorphism．High variation existed for protein or protein subunits with molecular weight 54-47kDa, 45-25kDa and 16-11kDa. The electrophoregram showed variation for globulin as well as other protein fractions．About 300 proteins were separated by two-dimensional electrophoresis(2-DE)in a common buckwheat(Fagopyrum esculentura Moench．)seed．Seed maturation is a dynamic and temporally regulated phase of seed development that determines the composition of storage reserves in mature seeds．Buckwheat sePAls from 5, 10, 15, 20, and 25 days after pollination and matured stage were used for the analysis．More than 300 protein spots could be detectable on a two-dimensional gel electrophoresis. This led to the establishment of high-resolution proteome reference maps, expression profiles of 50 spots．Our results will be useful for the future examination of the complex nature of protein expression during seed maturation in buckwheat. In the future, specific protein spots will be selected and in-gel digested for MS or MS／MS analysis．
Proteomic approach Buckwheat seed
Min-Hwa Park Adachi Taiji Sun-Hee Woo Seung-Woo Cho Ki-Na Yun Keun-Yook Chung Jong-Soon Choi Chul-Ho Parkd Hong-Sig Kim Seung-Keun Jong Clayton Campbell
Dept.of Crop Science, Chungbuk National University, Cheongju 361-763, KOREA KADE Research Ltd, 135-13 Street, Morden, Manitoba, R6M IE9, Canada Dept.of Agricultural Chemistry, ChungbukNational University, Cheongiu 361-763, KOREA Proteomics Analysis Team, Korea Basic Science Institute.Daejeon 305-333, KOREA College of Agriculture and Life Sciences, Kangwon National University, Chunchon 200-701, KOREA Center for Advanced Science and Innovation, Osaka University, Osaka, 567-0087 JAPAN