Production in Escherichia coli of biologically active secretin, a gastrointestinal hormone.
AUTOR(ES)
Suzuki, M
RESUMO
A synthetic gene for porcine secretin was ligated with Pst I-cleaved pBR322 by its flanking synthetic Pst I linkers to produce a fused protein consisting of an amino-terminal portion of beta-lactamase and an entire secretin molecule. The hybrid plasmid was transferred into competent Escherichia coli cells. The plasmids, which were proved in our investigation to contain the secretin gene in the desired orientation, were then screened for the production of secretin. This was shown by radioimmunoassay and gel electrophoretic analysis of the polypeptides that were synthesized in E. coli minicells transformed with the hybrid plasmids. Secretin so produced, whose carboxy terminal residue may not be amidated in contrast with natural porcine secretin, showed the same activity in stimulating pancreatic secretion in a bioassay with anesthetized rats as does natural secretin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=346221Documentos Relacionados
- High-level production of biologically active human alpha 1-antitrypsin in Escherichia coli.
- Endotoxin-free Biologically Active Component of Escherichia coli
- The expression of biologically active cholera toxin in Escherichia coli.
- Metabolic clearance of biologically active luteinizing hormone in man.
- The release of biologically active secretin-like immunoreactivity into duodenal lumen of dogs.