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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
 
 
 
 

Expression of biologically active recombinant-derived chicken prolactin in Escherichia coli.

The putative chicken prolactin (chPRL) cDNA clone PRL101 was manipulated in vitro and cloned into the Escherichia coli expression vector pKK2332 to produce a plasmid coding for recombinant-derived mature chPRL (R-chPRL). Expression of this manipulated cDNA sequence in E. coli resulted in the production of a 23 kDa protein which cross-reacted with specific chPRL antisera in Western blots. The partially purified protein stimulated ring dove crop sac mucosa to proliferate in a PRL bioassay, demonstrating that the R-chPRL was biologically active. R-chPRL was expressed at a level of approximately 1.5% of total cell protein.[1]

References

  1. Expression of biologically active recombinant-derived chicken prolactin in Escherichia coli. Hanks, M.C., Talbot, R.T., Sang, H.M. J. Mol. Endocrinol. (1989) [Pubmed]
 
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