STRUCTURE-FUNCTION RELATIONSHIPS OF SOYBEAN DOUBLE-HEADED PROTEINASE INHIBITORS

作者: Tokuji Ikenaka , Shoji Odani

DOI: 10.1016/B978-0-08-022628-6.50023-3

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摘要: Publisher Summary This chapter discusses the structure–function relationships of soybean double-headed proteinase inhibitors. Many natural inhibitors inhibit more than one at same time, and are called multi-headed The most extensively investigated legume origin, which can bind two proteinases their dual independent reactive sites. soybeans used for purification Sode-furi variety, cropped in 1973. Soybean meals were extracted with 60% ethanol room temperature inhibitor fraction was precipitated by adding a double volume cold acetone. sticky precipitates collected, dissolved water, dialyzed against water. Fraction A found to be BBI its chromatographic behavior, inhibitory pattern, amino acid composition purified materials. B on DE-32 column using ammonium acetate buffer system according Frattali. C first DEAE-cellulose column. Two major fractions, C-I C-II, obtained. C-II further SP-Sephadex C-25 chromatography finally chromatography.

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