%0 Journal Article
%T Bone-Inducing Activity of Human Bone Morphorgenetic Protein-2 102 Peptide<br>人骨形成蛋白-2C端102肽的诱骨活性
%A ZHANG Bin PU Qin ZHU Bang-Fu CHEN Nan-Chun CHEN Su-Min
%A <br>张斌
%A 蒲勤
%A 朱帮福
%A 陈南春
%A 陈苏民
%J 生物工程学报
%D 2001
%I 
%X To analyze the bone-inducing activity of C terminal of hBMP-2 and get a new recombinant product of hBMP-2, the gene encoding 102 aa of hBMP-2 mature peptide C terminal was cloned and expressed in E. coli and the first Cys was mutated with Ser. The fragments encoding the target peptide were amplified and cloned into heat-inducible expression vector pDH and transformed into E. coli DH5 alpha. After induction, a new protein bond appeared on the SDS-PAGE. The expressed products amounted to 30% of the total bacterial protein, which existed in the form of inclusion body. The products of bacterial lysates were purified through the ion-exchange chromatography. The denatured proteins were dialysed and diluted directly into the refolding buffer. The renatured products were implanted into mouse thigh muscles to analyze their bone-inducing activity respectively. The results of histological assay showed that the 102 peptide of hBMP-2 could ectopically induce formation of bone, while the mutated 102 peptide of hBMP-2 could not. It suggested hBMP-2 102 peptide still had bone-inducing activity. The first Cys of hBMP-2 mature peptide might be necessary for integrity of three pairs of disulfide bond, and also essential for bone-inducing activity of hBMP-2.
%K human bone morphogenetic protein-2(hBMP-2)
%K 102 peptide
%K bone-inducing activity<br>人骨形成蛋白-2
%K 102肽
%K 诱骨活性
%U http://www.alljournals.cn/get_abstract_url.aspx?pcid=90BA3D13E7F3BC869AC96FB3DA594E3FE34FBF7B8BC0E591&jid=A66E90C274451689E69F6F0291467824&aid=64B7ED7FC2D939A3&yid=14E7EF987E4155E6&vid=BCA2697F357F2001&iid=B31275AF3241DB2D&sid=DA280A426E11FC95&eid=6D25DD85174CF6DB&journal_id=1000-3061&journal_name=生物工程学报&referenced_num=0&reference_num=9