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Expression of biologically active recombinant-derived chicken prolactin in Escherichia coli
M C Hanks1, R T Talbot, H M Sang
1AFRC Institute of Animal Physiology and Genetics Research, Roslin, Midlothian.
Journal of Molecular Endocrinology
|July 1, 1989
Abstract:
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.