Abstract
DPR, a fragment peptide of enterostatin (VPDPR) having hypocholesterolemic activity, was introduced into the three homologous sites, EPR, DYR, and DPI, in the soybean β-conglycinin α′ subunit by site-directed mutagenesis. The modified β-conglycinin was expressed in Escherichia coli and recovered in the soluble fraction. After purification on ion-exchange HPLC, the modified β-conglycinin was digested by trypsin to release integrated DPR. The yield of DPR from 1 mole of the modified β-conglycinin was 1.2 mole.
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Takenaka, Y., Doyama, N., Maruyama, N., Utsumi, S., & Yoshikawa, M. (2004). Introduction of DPR, an enterostatin fragment peptide, into soybean β-conglycinin α′ subunit by site-directed mutagenesis. Bioscience, Biotechnology and Biochemistry, 68(1), 253–256. https://doi.org/10.1271/bbb.68.253
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