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- W1963964562 abstract "A protein fraction was isolated from defatted soybean flour by extraction at acid pH, 40% ammonium sulfate precipitation, hydrophobic interaction chromatography, and gel filtration chromatography. SDS–PAGE, under reducing conditions, confirmed it as a homogeneous preparation. This conclusion was consistent with N-terminal amino acid sequence data (20 cycles) which showed a major sequence identical to those reported for soybean Bowman–Birk-type protease inhibitor (BBI), and also indicated a minimum 95% purity based on recoveries of PTH-amino acid residues. The purified fraction inhibited both trypsin and chymotrypsin with average specific activities of 350 and 672 units mg−1, respectively. Compared with classical BBI purification, this procedure is very rapid requiring only 72–96 h to achieve a yield of 37 mg purified BBI per 200 g starting material." @default.
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- W1963964562 date "1996-05-01" @default.
- W1963964562 modified "2023-09-27" @default.
- W1963964562 title "A Rapid Purification Method for Soybean Bowman–Birk Protease Inhibitor Using Hydrophobic Interaction Chromatography" @default.
- W1963964562 doi "https://doi.org/10.1006/prep.1996.0044" @default.
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