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• W1964329395 startingPage "621" @default.
• W1964329395 abstract "A dimeric 70-kDa chymotrypsin inhibitor with substantial N-terminal sequence homology to serine protease inhibitors was isolated from Acacia confusa seeds. The chymotrypsin inhibitor was purified using a protocol that entailed ion exchange chromatography on Q-Sepharose, SP-Sepharose and fast protein liquid chromatography-gel filtration on Superdex 75. The chymotrypsin inhibitor was unadsorbed on both Q-Sepharose and SP-Sepharose. Its chymotrypsin inhibitory activity was stable from pH 3 to 10 and from 0 to 50 °C. It exerted antiproliferative activity toward breast cancer MCF-7 cells with an IC50 of 10.7±4.2 μM. It inhibited HIV-1 reverse transcriptase with an IC50 of 8±1.5 μM. It was devoid of antifungal activity toward a variety of fungal species. The distinctive features of the chymotrypsin inhibitor included dimeric nature, a high molecular mass, lack of trypsin inhibitory activity, highly potent HIV-1 reverse transcriptase inhibitory activity, specific antitumor activity and relatively high pH-stability." @default.
• W1964329395 created "2016-06-24" @default.
• W1964329395 creator A5035780833 @default.
• W1964329395 creator A5084951997 @default.
• W1964329395 date "2010-07-01" @default.
• W1964329395 modified "2023-09-23" @default.
• W1964329395 title "A dimeric high-molecular-weight chymotrypsin inhibitor with antitumor and HIV-1 reverse transcriptase inhibitory activities from seeds of Acacia confusa" @default.
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• W1964329395 doi "https://doi.org/10.1016/j.phymed.2009.10.005" @default.
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