PubMed:762150 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PubMed/sourceid/762150","sourcedb":"PubMed","sourceid":"762150","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/762150","text":"Purification of pre-prolactin mRNA from bovine anterior pituitary glands.\nTotal cytoplasmic RNA, isolated from bovine anterior pituitary glands, directed the synthesis of primarily two proteins in a wheat germ cell-free system. Analysis of wheat germ cell-free products by sodium dodecyl sulfate-slab gel electrophoresis, direct immunoprecipitation with prolactin aatibody, and prolactin- and growth hormone-specific radioimmunoassay indicated that the two proteins were pre-prolactin and pre-growth hormone. Agarose-urea-gel electrophoresis of poly(A)-containing RNA revealed the presence of a large symmetrical RNA peak with an estimated size of approximately 15 S. The RNA contained in this peak was eluted from the gel and translated in the wheat germ cell-free system. Analysis of the translation products by electrophoresis, direct immunoprecipitation, and radioimmunoassay resulted in the detection of only pre-prolactin. The extent of pre-prolactin mRNA purification was assessed by synthesizing DNA complementary to gel-purified pre-prolactin mRNA and then following the hybridization of this cDNA to gel purified pre-prolactin mRNA. The result of this hybridization is consistent with the cell-free translation studies, namely that pre-prolactin mRNA is the predominant mRNA component of pituitary poly(A)-containing 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