Cloning, purification and biological activity of human vascular endothelial growth factor fragment in E. coli / 中华肿瘤杂志
Chinese Journal of Oncology
; (12): 448-450, 2002.
Article
in Zh
| WPRIM
| ID: wpr-301991
Responsible library:
WPRO
ABSTRACT
<p><b>OBJECTIVE</b>To observe the effect of human vascular endothelial growth factor (VEGF) fragment (3 approximately 4 exon) in E. coli on anti-angiogenesis.</p><p><b>METHODS</b>Through RT-PCR amplification, endonuclease cut and DNA sequence analysis identification, hVEGF fragment cDNA was inserted into E. coli expression vector pTrcHis2A. The prokaryotic expression plasmid pTrcHis2A/VEGF(3 approximately 4) was constructed and transformed into TOP10F.</p><p><b>RESULTS</b>After 8hr isopropy-beta-D-thiogalactoside (IPTG) induction, VEGF fragment was expressed in 15% of total proteins through sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The expressed protein was highly antigenic and specific. The VEGF fragment was further purified by affinity, which could inhibit HUVEC proliferation and neovascularization of the chick chorioallantoic membrane.</p><p><b>CONCLUSION</b>VEGF fragment is anti-angiogenetic, which may potentially be used in oncologico-biological targeting therapy.</p>
Full text:
1
Index:
WPRIM
Main subject:
Peptide Fragments
/
Pharmacology
/
Plasmids
/
Gene Expression
/
Polymerase Chain Reaction
/
Endothelial Growth Factors
/
Lymphokines
/
Cloning, Molecular
/
Angiogenesis Inhibitors
/
Intercellular Signaling Peptides and Proteins
Type of study:
Prognostic_studies
Limits:
Humans
Language:
Zh
Journal:
Chinese Journal of Oncology
Year:
2002
Type:
Article