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A novel ribonuclease with potent HIV-1 reverse transcriptase inhibitory activity from cultured mushroom Schizophyllum commune

文献类型： 外文期刊

作者： Zhao, Yong-Chang 3 ; Zhang, Guo-Qing 1 ; Ng, Tzi-Bun 5 ; Wang, He-Xiang 1 ;

作者机构： 1.China Agr Univ, State Key Lab Agrobiotechnol, Beijing 100193, Peoples R China

2.China Agr Univ, Dept Microbiol, Beijing 100193, Peoples R China

3.Yunnan Acad Agr Sci, Inst Biotechnol & Germplasm Resource, Kunming 650223, Peoples R China

4.China Agr Univ, Key Lab Urban Agr N, Minist Agr, Beijing 102206, Peoples R China

5.Chinese Univ Hong Kong, Dept Biochem, Fac Med, Shatin, Hong Kong, Peoples R China

关键词： mushroom;purification;ribonuclease;Schizophyllum commune

期刊名称：JOURNAL OF MICROBIOLOGY （ 影响因子：3.422； 五年影响因子：3.28 ）

ISSN：

年卷期：

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收录情况： SCI

摘要： A 20-kDa ribonuclease (RNase) was purified from fresh fruiting bodies of cultured Schizophyllum commune mushrooms. The RNase was not adsorbed on Affi-gel blue gel but adsorbed on DEAE-cellulose and CM-cellulose. It exhibited maximal RNase activity at pH 6.0 and 70°C. It demonstrated the highest ribonucleolytic activity toward poly (U) (379.5 μ/mg), the second highest activity toward poly (C) (244.7 μ/mg), less activity toward poly (A) (167.4 μ/mg), and much weaker activity toward poly (G) (114.5 μ/mg). The RNase inhibited HIV-1 reverse transcriptase with an IC_(50) of 65 μM. No effect on [~3H-methyl]-thymidine uptake by lymphoma MBL2 cells and leukemia L1210 cells was observed at 100 μM concentration of the RNase. A comparison of RNases from S. commune and Volvariella volvacea revealed that they demonstrated some similarities in N-terminal amino acid sequence, optimum pH and polyhomoribonucleotide specificity. However, some differences in chromatographic behavior and molecular mass were observed.

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