Abstract
RNA prepared from rat anterior pituitaries or from prolactin secreting pituitary tumors has been shown to direct the synthesis of a large form of prolactin in a cell free system derived from wheat germ. Immunoprecipitation of cell free reactions demonstrated the synthesis of a product which was recognized by a specific antiprolactin antisera. Analysis of the immunoprecipitate on sodium dodecyl sulfate containing polyacrylamide gels suggested that the cell free product has a molecular weight of approximately 28,000 compared to 22,500 for prolactin. RNA prepared by completely different techniques from rat pituitary and a pituitary tumor resulted in identical large translation products. Translation of tumor RNA in a cell free system from Krebs ascites cells also resulted in a similar large product. The identity of the cell free product as prolactin was confirmed by comparing peptides derived from the cell free product and prolactin. The results of these studies suggest that prolactin messenger RNA directs the cell free synthesis of a product which contains the amino acid sequence of prolactin but which has an addition at one or both ends of the molecule.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 2801-2807 |
| Number of pages | 7 |
| Journal | Journal of Biological Chemistry |
| Volume | 251 |
| Issue number | 9 |
| State | Published - 1976 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Biochemistry
Cite this
Cell free synthesis of a large translation product of prolactin messenger RNA. / Maurer, Richard; Stone, R.; Gorski, J.
In: Journal of Biological Chemistry, Vol. 251, No. 9, 1976, p. 2801-2807.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Cell free synthesis of a large translation product of prolactin messenger RNA
AU - Maurer, Richard
AU - Stone, R.
AU - Gorski, J.
PY - 1976
Y1 - 1976
N2 - RNA prepared from rat anterior pituitaries or from prolactin secreting pituitary tumors has been shown to direct the synthesis of a large form of prolactin in a cell free system derived from wheat germ. Immunoprecipitation of cell free reactions demonstrated the synthesis of a product which was recognized by a specific antiprolactin antisera. Analysis of the immunoprecipitate on sodium dodecyl sulfate containing polyacrylamide gels suggested that the cell free product has a molecular weight of approximately 28,000 compared to 22,500 for prolactin. RNA prepared by completely different techniques from rat pituitary and a pituitary tumor resulted in identical large translation products. Translation of tumor RNA in a cell free system from Krebs ascites cells also resulted in a similar large product. The identity of the cell free product as prolactin was confirmed by comparing peptides derived from the cell free product and prolactin. The results of these studies suggest that prolactin messenger RNA directs the cell free synthesis of a product which contains the amino acid sequence of prolactin but which has an addition at one or both ends of the molecule.
AB - RNA prepared from rat anterior pituitaries or from prolactin secreting pituitary tumors has been shown to direct the synthesis of a large form of prolactin in a cell free system derived from wheat germ. Immunoprecipitation of cell free reactions demonstrated the synthesis of a product which was recognized by a specific antiprolactin antisera. Analysis of the immunoprecipitate on sodium dodecyl sulfate containing polyacrylamide gels suggested that the cell free product has a molecular weight of approximately 28,000 compared to 22,500 for prolactin. RNA prepared by completely different techniques from rat pituitary and a pituitary tumor resulted in identical large translation products. Translation of tumor RNA in a cell free system from Krebs ascites cells also resulted in a similar large product. The identity of the cell free product as prolactin was confirmed by comparing peptides derived from the cell free product and prolactin. The results of these studies suggest that prolactin messenger RNA directs the cell free synthesis of a product which contains the amino acid sequence of prolactin but which has an addition at one or both ends of the molecule.
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UR - http://www.scopus.com/inward/citedby.url?scp=0017118515&partnerID=8YFLogxK
M3 - Article
VL - 251
SP - 2801
EP - 2807
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 9
ER -