Ultracentrifugal and Electrophoretical Studies on Common Bean (Phaseolus vulgaris) Protein
スポンサーリンク
概要
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P. vulgaris seed protein was extracted with 85-95% efficiency, mildly without precipitation or low ionic treatment. No distinct 11-12S, 28S, nor 33S (which were reported before) was observed by ultracentrifuge analyses of 11 varieties. The main components, 7S and 18-19S in acidic solutions, were separated with Sepharose 6B chromatography into peak 2 (P2) and peak 1 (P1), respectively. P1 seemed to correspond to G1 (one of P. vulgaris main proteins). Following DEAE-Sepharose chromatography eliminated a part of the minor components from P1. Sedimentation coefficients, dissociation-association behavior, and molecular weight of P1 were studied.
著者
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YANAGI Sonoe
National Food Research institute, Ministry of Agriculture, Forestry and Fisheries
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Matsukura Ushio
National Agriculture And Food Research Organization (naro) National Institute Of Crop Science:nation
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Yanagi Sonoe
National Food Research Institute
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KITO Masako
National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries
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GALEAZZI Maria
Faculty of Food Engineering and Agriculture, University of Campinas, Cidade Universitaria
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MATSUKURA Ushio
National Food Research Institute, Ministry of Agriculture, Forestry and Fisheries
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