Cloning and expression of a porcine prorelaxin gene in E. coli.

A porcine prorelaxin gene has been constructed partly by synthetic means and partly from its natural messenger RNA. A gene coding for the 32 N-terminal amino acids including a chain initiator methionine codon (B gene) was synthesised and inserted in a plasmid at a site downstream from a tryptophan promoter in such a way that its expression is under the control of the trp promoter. DNA corresponding to the rest of the prorelaxin was prepared using reverse transcriptase extension of a primer complementary to relaxin mRNA and joined at a suitable restriction site to the B gene. Transformation of E. coli with this plasmid followed by suitable induction resulted in the synthesis of a new protein identified as prorelaxin by its size and its antigenic similarity to relaxin.