[Isolation and characterization of prolactin messenger RNA from bovine anterior pituitary glands]

The messenger RNA was extracted from bovine anterior pituitary glands and was purified by oligo(dT)-cellulose chromatography. The length of the mRNA was 1,200 nucleotides measured by agarose gel electrophoresis containing methylmercury hydroxide. The bovine prolactin (PRL) mRNA was confirmed by Northern blot analysis of the mRNA with gamma-32P labelled synthetic oligonucleotide probes based on the partial amino acid sequences of bovine PRL and could stimulate the incorporation of 35S-methionine into protein in the rabbit reticulocyte cell-free system. The translation product of bovine PRL mRNA was immunoprecipitable by rabbit anti-ovine PRL anti-antibodies. The molecular weight of the translation product corresponding to the bovine PRL precursor was estimated to be approximately 25,000 by SDS polyacrylamide gel electrophoresis and autoradiograph.