title: Chemical synthesis and expression of the human calcitonin gene.
abstract: A gene coding for the peptide hormone, human calcitonin (hCT), has been constructed and expressed in bacteria using a prokaryotic vector containing the strong T5P25 promoter and a strong ribosome-binding site. The bacterial hCT is different from the natural hCT by having an additional Met residue at the N terminus and a non-amidated C terminus. Despite these differences, the bacterial hCT is biologically active in rat cells. The results are important for future structure-function relationship studies using mutants constructed by genetic engineering.
authors.affiliation: Department of Chemistry, University of New Brunswick, Fredericton, Canada.
authors.forename: I
authors.initials: I
authors.lastname: Ivanov
authors.forename: J
authors.initials: J
authors.lastname: Tam
authors.forename: P
authors.initials: P
authors.lastname: Wishart
authors.forename: E
authors.initials: E
authors.lastname: Jay
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D002116:Calcitonin / Q000235:genetics* / Q000494:pharmacology; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D005796:Genes; D006801:Humans; D008297:Male; D008969:Molecular Sequence Data; D010957:Plasmids; D011401:Promoter Regions, Genetic; D051381:Rats; D011919:Rats, Inbred Strains; D014158:Transcription, Genetic
chemical_list: D002116:Calcitonin