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    科研论文:Purification and characterization of a ribonuclease from the wild edible mushroom Armillaria luteo-virens.

    发布时间:2014-04-16 17:48:08 责任编辑: 点击次数:

     

    Indian Journal of Biochemistry & Biophysics, Vol. 50, June 2013, pp. 196-201

     

    Purification and characterization of a ribonuclease from the wild edible mushroom Armillaria luteo-virens.

     

    Xu LJ, Chen QJ, Wang HX, Zhang GQ.

     

    A 15 kDa ribonuclease (RNase) was purified from dried fruiting bodies of the wild edible mushroom Armillaria luteo-virens. The simple 4-step purification protocol involved ion-exchange chromatography on DEAE-cellulose, affinity chromatography on Affi-gel blue gel, ion-exchange chromatography on SP-Sepharose and a final gel filtration by FPLC on Superdex-75. The RNase was unadsorbed on Affi-gel blue gel, but adsorbed on DEAE-cellulose and SP-Sepharose. The N-terminal amino acid sequence of purified RNase was AGVQYKLTILLV, which showed low sequence homology to those of previously reported RNases. The optimal pH and temperature of the enzyme were very close to 4.0 and 70 degrees C, respectively. The enzyme showed considerably high ribonucleolytic activity and broad specificity towards polyhomoribonucleotides, with a specificity of poly(U) > poly(C) > poly (G) > poly(A). The ribonucleolytic activities towards poly(U), poly(C), poly(G) and poly(A) were 279.5, 184.1, 69.9 and 52.3 U/mg, respectively.

     

    Keywords: Armillaria luteo-virens, Muchroom, Purification, Ribonuclease

     

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