Font Size: a A A

The Expression, Purification And Renaturation Of The Mature Peptide Of HBMP-2 In E.Coli And Its Biological Activities

Posted on:2001-07-20Degree:DoctorType:Dissertation
Country:ChinaCandidate:Q PuFull Text:PDF
GTID:1100360185496737Subject:Biochemistry and Molecular Biology
Abstract/Summary:PDF Full Text Request
Bone morphogenetic protein-2 (BMP-2) plays a decisive role during bone regeneration and repair as well as during various stages of embryonal development. The complete cDNA of human bone morphogenetic protein-2 (hBMP-2) is 1587bp long, and the 1188bp open reading frame encodes a 396aa protein which consists of a signal peptide, a pro-peptide and a 114 aa mature peptide. The recombinant hBMP-2 was expressed in COS, CHO and insect cells as a functional active form. Liu xin ping, Lu zifan, Zhao ming and Lin song et al expressed varied C-terminal peptides of hBMP-2 in E.coli respectively, and after purification and renaturation the rBMPs was prepared as a functional active form. In this paper, the cDNA encoding the mature peptide of hBMP-2 was cloned and expressed in E.coli.The cDNA fragment encoding the mature peptide of hBMP-2m was amplified with PCR and inserted into two heat-inducible expression vectors pDHEX and pDHEEX in which foreign gene is controlled by P_RP_L promoters. E.coli DH5α transformed with...
Keywords/Search Tags:human bone morphogenetic protein-2(hBMP-2), Genetic engineering, Escherichia coli, High cell-density culture of Escherichia coli, Protein purification, Refoldding, Bone-inducing activity, Haematogenesis
PDF Full Text Request
Related items