A Novel Aspartic Protease with HIV-1 Reverse Transcriptase Inhibitory Activity from Fresh Fruiting Bodies of the Wild Mushroom Xylaria hypoxylon

文献类型： 外文期刊

第一作者： Hu, Qing-Xiu

作者： Hu, Qing-Xiu;Wang, He-Xiang;Hu, Qing-Xiu;Wang, He-Xiang;Hu, Qing-Xiu;Zhang, Rui-Ying;Zhang, Guo-Qing;Hu, Dan-Dan;Ng, Tzi Bun

作者机构：

期刊名称：JOURNAL OF BIOMEDICINE AND BIOTECHNOLOGY （ 影响因子：3.169； 五年影响因子：3.132 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： A novel aspartic protease with HIV-1 RT inhibitory activity was isolated and characterized from fruiting bodies of the wild mushroom Xylaria hypoxylon. The purification protocol comprised distilled water homogenization and extraction step, three ion exchange chromatographic steps (on DEAE-cellulose, Q-Sepharose, and CM-cellulose in succession), and final purification was by FPLC on Superdex 75. The protease was adsorbed on all the three ion exchangers. It was a monomeric protein with a molecular mass of 43 kDa as estimated by SDS-PAGE and FPLC. Its N-terminal amino acid sequence was HYTELLSQW, which exhibited no sequence homology to other proteases reported. The activity of the protease was adversely affected by Pepstatin A, indicating that it is an aspartic protease. The protease activity was maximal or nearly so in the pH range 6-8 and in the temperature range 35-60degC. The purified enzyme exhibited HIV-1 RT inhibitory activity with an IC50 value of 8.3 fiM, but was devoid of antifungal, ribonuclease, and hemagglutinating activities.

分类号： R3

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