Affiliation:
1. School of Biomedical Sciences, Faculty of Medicine, The Chinese University of Hong Kong, Shatin New Territories, Hong Kong
Abstract
Protease inhibitors (PIs) and hemagglutinins are defense proteins produced by many organisms. From Chinese mini-black soybeans, a 17.5-kDa PI was isolated using chromatography on Q-Sepharose, SP-Sepharose, and DEAE-cellulose. A 25-kDa hemagglutinin was purified similarly, but using Superdex 75 instead of DEAE-cellulose in the final step. The PI inhibited trypsin and chymotrypsin (IC50= 7.2 and 8.8 μM). Its trypsin inhibitory activity was stable from pH 2 to pH 13 and from 0∘C to 70∘C. The hemagglutinin activity of the hemagglutinin was stable from pH 2 to pH 13 and from 0∘C to 75∘C. The results indicated that both PI and hemagglutinin were relatively thermostable and pH-stable. The trypsin inhibitory activity was inhibited by dithiothreitol, signifying the importance of the disulfide bond to the activity. The hemagglutinating activity was inhibited most potently by D (+)-raffinose and N-acetyl-D-galactosamine, suggesting that the hemagglutinin was specific for these two sugars. Both PI and hemagglutinin inhibited HIV-1 reverse transcriptase (IC50= 3.2 and 5.5 μM), proliferation of breast cancer cells (IC50= 9.7 and 3.5 μM), and hepatoma cells (IC50= 35 and 6.2 μM), with relatively high potencies.
Subject
Complementary and alternative medicine
Cited by
16 articles.
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