%0 Journal Article
%T Purification and Structural Analysis of The Nucleocapsid of PRRS Virus Expressed from Escherichia coli<br>猪繁殖与呼吸综合征病毒N蛋白的原核表达、纯化与结构分析
%A Jin-Hai Huang
%A Han-Chun Yang
%A Xin Guo
%A Yan-Hong Chen
%A Zhen-Lin Zha
%A <br>黄金海
%A 杨汉春
%A 郭鑫
%A 陈艳红
%A 查振林
%J 微生物学报
%D 2004
%I 
%X The DNA fragment encoding the nucleocapsid protein (N) of PRRSV BJ4 strain were cloned into the BamH I / EcoR I sites of pET28a vector to construct the expression plasmid pET28-N by designing special primers. The soluble protein (P28-N) were obtained by introducing the expression plasmid into E. coli BL21 (DE3) host cell, and the amount of recombinant protein reached to 28% of the total mass of bacterial protein. PET28-N were purified by nickel-affinity column of Proband resin. The circular dichroism (CD) analysis showed that the purified PET28-N shared a significant (26%) alpha-helical structure, beta-sheet (23.7%), beta-turn (19.8%), and random coil (30.3%), respectively. Finally,the secondary structure of N protein of PRRSV was deduced.
%K PRRSV
%K Nucleocapsid protein
%K Circular dichroism (CD)
%K Secondary stucture<br>猪繁殖与呼吸综合征病毒
%K N蛋白
%K 圆二色谱
%K 二级结构
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=DF3B7082111C56B0&yid=D0E58B75BFD8E51C&vid=1AE5323881A5ECDC&iid=B31275AF3241DB2D&sid=8CC50269EED5BB47&eid=3EE58D91F4253193&journal_id=0001-6209&journal_name=微生物学报&referenced_num=0&reference_num=18