人乳铁蛋白阳离子多肽重组Taq DNA聚合酶的研究  

Study on modification of Taq DNA polymerase by replacing of its N-terminal 289 amino acids with cationic peptide of human lactoferrin

作　　者：何绍宗 齐文川 李晓杰[1] 曾凡亚[1] 

机构地区：[1]四川大学生命科学学院,成都610064

出　　处：《四川大学学报（自然科学版）》2016年第3期633-638,共6页Journal of Sichuan University(Natural Science Edition)

摘　　要：本文报道了人乳铁蛋白阳离子多肽(HL-N)替换Taq DNA聚合酶N-末端结构域,构建新型重组Taq酶的研究结果.利用合成寡核苷酸,成功获得具DNA合成功能的HL-N重组Taq酶.对该重组酶的DNA合成加工、血清耐受性等测试显示,HL-N重组Taq DNA聚合酶的DNA扩增速度、扩增物产量、以及对反应体系中血清浓度的耐受性都得到显著提高.Taq DNA polymerase consists of isolated functional domains responsible for binding of template DNA and catalysis of DNA synthesis,respectively.In the present study,a recombinant Taq DNA polymerase was constructed by replacing the N-terminal 289 amino acids of Taq DNA polymerase with cationic peptide of human lactoferrin（NL-N）.Some enzymatic properties of the chimerical recombinant DNA polymerase,such as the processivity,5′→3′exonuclease activity,and tolerance to serum concentration in PCR reaction system,were characterized experimentally and the testing data showed that the modification of DNA-binding domain with NL-N improved the polymerase in several aspects.

关 键 词：TAQ DNA聚合酶 人乳铁蛋白 基因工程 PCR 

分 类 号：Q812[生物学—生物工程]