%0 Journal Article
%T Purification and Some Properties of D-Carbamoylase<br>N-氨甲酰基-D-氨基酸酰胺水解酶的快速纯化及性质
%A Yuan Jingming
%A Shi Yawei
%A Yang Xiuqing
%A <br>袁静明
%A 石亚伟
%A 杨秀清
%A 连惠勇
%A 齐延红
%J 微生物学报
%D 2002
%I 
%X A D-Carbamoylase produced by a strain NO. 2262 was purified to electrophoretic homogeneity with the recovery of 20% activity and the purification factor of 8 fold by three steps including (NH4)2SO4 fractionation, hydrophobic column and pre-packed Hitrap Q HR. It is indicated from the results of nativ-PAGE and SDS-PAGE analysis that the enzyme could be a homogeneous tetramer consisting of four 35 kD subunits. In addition, its optimal pH and optimal temperature are 8.0 and 45 degrees C respectively. The basic kinetic parameters of the enzyme are Km = 1.3 x 10(-3) mol/L and Vmax = 0.33 mumol/min with N-carbamyl-DL-Alanine as the substrate. The effect of bivalent metal ions on the enzyme was showed that Ni2+ could be as an activator, Zn2+ as a powerful inhibitor, while Co2+ had no any influence at all. Its N-terminal sequence is TRQKILAF in turn.
%K Strain No
%K 2262
%K D-Carbamoylase
%K Purification
%K Properties<br>菌株NO.2262
%K N－氨甲酰基－D－氨基酸酰胺水解酶
%K 纯化
%K 性质
%K D－氨基酸
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=41EF25D04DF7BFB5&yid=C3ACC247184A22C1&vid=ECE8E54D6034F642&iid=CA4FD0336C81A37A&sid=7E8E8B150580E4AB&eid=08805F9252973BA4&journal_id=0001-6209&journal_name=微生物学报&referenced_num=4&reference_num=11