Preliminary study on the cleavage of fusion protein GST-CMIV with palladium(II) complex.
A novel method for post-treatment of gene-engineered proteins is reported. A coden of Cys-His unit is introduced into the N-terminal of cecropin CMIV by using PCR. The gene is expressed in E. coli fused with GST. After purification, the fusion protein is cleaved by [Pd(en)(H2O)2]2+ at the His-Arg bond and the cecropin CMIV with antibacterial activity is obtained. The preliminary results held some promise of success for application of the palladium(II) complex as cleavage agent for the production of peptide drugs from gene-engineering fusion proteins.
Dou
F
F
Department of Biochemistry Nanjing University, PR China.
Qiao
F
F
Hu
J
J
Zhu
T
T
Xu
X
X
Zhu
D
D
Zhu
L
L
D000900:Anti-Bacterial Agents / Q000378:metabolism / Q000494:pharmacology; D004926:Escherichia coli; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D019476:Insect Proteins / Q000737:chemistry* / Q000235:genetics / Q000494:pharmacology; D010165:Palladium / Q000378:metabolism*; D010446:Peptide Fragments / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D010957:Plasmids / Q000235:genetics; D015202:Protein Engineering; D011993:Recombinant Fusion Proteins / Q000378:metabolism / Q000494:pharmacology
D000900:Anti-Bacterial Agents; D019476:Insect Proteins; D010446:Peptide Fragments; D011993:Recombinant Fusion Proteins; C405946:cecropin CMIV protein, Bombyx mori; D010165:Palladium; D005982:Glutathione Transferase