Chemical synthesis and expression of the human calcitonin gene.
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.
Ivanov
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I
Department of Chemistry, University of New Brunswick, Fredericton, Canada.
Tam
J
J
Wishart
P
P
Jay
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E
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
D002116:Calcitonin