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污白干酪菌核糖核酸酶的分离纯化和理化性质

Purification and Characterization of Ribonuclease from Tyromyces amygdalinus

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【作者】 耿雪冉柳万石王贺祥

【Author】 GENG Xue-ran;Ryu Mansok;WANG He-xiang;State Key Laboratory for Agrobiotechnology and Department of Microbiology, College of Biologial Sciences, China Agricultural University;Pyongyang Kim Hyong Jik University of Education;

【机构】 中国农业大学生物学院农业生物技术国家重点实验室金亨稷师范大学

【摘要】 采用DEAE-cellulose阴离子交换层析、CM-cellulose阳离子交换层析和FPLC-Superdex-75凝胶过滤层析,从污白干酪菌(Tyromyces amygdalinus)干子实体纯化得到一种核糖核酸酶,SDS-PAGE电泳检测其为单一蛋白,分子量为25 k Da。最适反应条件为60℃,p H4.4。该酶对几种寡聚核糖核苷酸的水解活性低于对t-RNA的水解活性。

【Abstract】 A novel ribonuclease( RNase) was purified from dry fruit bodies of Tyromyces amygdalinus using a purification procedure which involved ion exchange chromatography on DEAE-cellulose, CM-cellulose and gel filteration chromatography by FPLC on superdex 75 HR 10/300 column. Combine with the result from FPLC and SDS-PAGE, it was estimated that this ribonuclease was a monomeric protein with a molecular weight of 25 k D. The optimum temperature of this RNase is 60℃, and optimum p H of it is 4.4. The activity of this enzyme toward poly A and poly C was lower than that of t-RNA.

【基金】 现代农业产业技术体系建设专项基金(CARS-24)
  • 【文献出处】 中国食用菌 ,Edible Fungi of China , 编辑部邮箱 ,2015年06期
  • 【分类号】Q936
  • 【被引频次】1
  • 【下载频次】102
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