%0 Journal Article
%T PURIFICATION AND GENE CLONING OF A NOVEL FIBRINOLYTIC PROTEASE FROM STREPTOMYCES SP. C3662
一种来源于链霉菌的纤溶酶的纯化及其基因的克隆
%A Gong Yong
%A Wang Yiguang
%A
龚勇
%A 王以光
%J 微生物学报
%D 2001
%I
%X A novel fibrinolytic protease from \%Streptomyces\% sp.C3662 was purified by (NH 4) 2SO 4 fractionation,DEAE\|Sepharose and CM\|Sepharose chromatography.The molecular weight of the protease was indicated to be 30 kD by SDS\|PAGE.Using a \%E.coli/Streptomyces\% shuttle plasmid pIJ699 as the vector,shot\|gun cloning was performed to clone the gene of the protease.One clone with fibrinolytic activity harboring a plasmid that contains a DNA fragment of 6kb was obtained from 3000 clones.Sequence analysis reveals that the open reading frame of the gene of the protease is 903bp in size,encoding a putative protein of 300 amino acids with 30kD.The overall GC% and the third codon GC% of the ORF were 68 33% and 956%,respectively.Comparison of homologue showed that the purative protein is highly homologous with other proteases of Streptomyces\sp.
%K Streptomyces sp
%K Fibrinolytic protease
%K Purification
%K Gene cloning
纤溶酶
%K 纯化
%K 鸟枪克隆
%K 链霉菌
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A3C6BA55AB623B90FA9104CFFC826F3C&aid=652D559205FD0E84&yid=14E7EF987E4155E6&vid=2001E0D53B7B80EC&iid=0B39A22176CE99FB&sid=50BBDFAC8381694B&eid=6235172E4DDBA109&journal_id=0001-6209&journal_name=微生物学报&referenced_num=1&reference_num=6