利用家蚕病毒颗粒表达和纯化抗肿瘤药物天冬酰胺酶  

Expression and purification of antitumor drug L-asparaginase with Bombyx mori virus particles

作　　者：王文兵[1] 孔莉[1] 施国方 吴岩[1] 白雪川 费建明 

机构地区：[1]江苏大学生命科学研究院,江苏镇江212013 [2]湖州农业科学研究院养蚕研究所,浙江湖州313000

出　　处：《江苏大学学报（医学版）》2013年第2期134-136,148,共4页Journal of Jiangsu University：Medicine Edition

基　　金：浙江省科技计划资助项目(2011C32005)

摘　　要：目的:通过家蚕病毒颗粒简化抗肿瘤药物L-天冬酰胺酶的生产纯化过程,为抗肿瘤的药物生产提供依据。方法:利用基因重组技术构建pFastdual-polh-da26-asp融合蛋白真核表达载体,利用杆状病毒表达系统在家蚕细胞中表达融合蛋白,奈氏试剂法检测L-天冬酰胺酶活性。结果:成功构建了重组表达载体,融合蛋白在家蚕细胞中顺利表达,并检测到L-天冬酰胺酶在家蚕细胞中表达,活性为2 113.52 U/mg。结论:重组病毒颗粒成功表达,且L-天冬酰胺酶具有一定的活性;可以利用家蚕颗粒病毒简化纯化抗肿瘤药物L-天冬酰胺酶。Objective： To simplify the production and purification process of antitumor drug L-asparaginase by Bombyx mori virus,and to provide the basis for drug production of tumor therapy.Methods： The pFastdual-polh-da26-asp fusion protien eukaryotic expression vector was constructed by gene recombination technique.The fusion protein was expressed by the baculovirus expression system in Bombyx mori cells.The activity of L-asparagine was detected by using nessler reagent.Results： The recombinant expression vector was constructed successfully;and the fusion protein was expressed in Bombyx mori cells.The activity of L-asparagine was 2 113.52 U/mg.Conclusion： The recombinant virus particles were expressed efficiently,and the product L-asparagine has certain activity.

关 键 词：家蚕 杆状病毒 da26 L-天冬酰胺酶 大肠埃希菌 

分 类 号：R73-36[医药卫生—肿瘤]