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.
Hanks
M C
MC
AFRC Institute of Animal Physiology and Genetics Research, Roslin, Midlothian.
Talbot
R T
RT
Sang
H M
HM
D000818:Animals; D000906:Antibodies; D001681:Biological Assay; D015153:Blotting, Western; D002645:Chickens / Q000235:genetics; D003001:Cloning, Molecular; D003426:Crop, Avian / Q000166:cytology / Q000187:drug effects; D003429:Cross Reactions; D004926:Escherichia coli / Q000235:genetics*; D010957:Plasmids; D011388:Prolactin / Q000096:biosynthesis / Q000235:genetics* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000235:genetics / Q000494:pharmacology
D000906:Antibodies; D011994:Recombinant Proteins; D011388:Prolactin