PMID: 6397077Nov 15, 1984Paper

Cleaving of disulfide bridges and apparent molecular weight of human prolactin variants as revealed by immunoperoxidase electrophoresis

Analytical Biochemistry
S MeurisC Robyn

Abstract

Five highly purified preparations of human pituitary prolactin, widely used in radioimmunoassays, were analyzed by immunoperoxidase electrophoresis with rabbit antisera raised against ovine and rat prolactin. When unreduced, the prolactin content of these preparations was separated into one major prolactin-like immunoreactive band of Mr 23,000, and four fainter immunoreactive bands of Mr's 16,000, 22,000, 25,000, and 45,000. Increasing the 2-mercaptoethanol concentration modified the relative proportions and the Mr of immunoreactive bands so that, after extensive reduction, only two immunoreactive bands were separated, one major band of Mr 25,000 and one fainter band of Mr 17,000. A direct relationship existed between the load of prolactin submitted to electrophoresis in the 0.25 to 75 ng range and the optical density of the separated bands.

References

Sep 1, 1979·Proceedings of the National Academy of Sciences of the United States of America·H TowbinJ Gordon
Dec 11, 1979·Biochimica Et Biophysica Acta·P RoosL Wide
Oct 1, 1976·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·P PetruszP DiMeo
Nov 1, 1977·The Journal of Clinical Endocrinology and Metabolism·B Shome, A F Parlow
Sep 1, 1971·Biochemical and Biophysical Research Communications·U J LewisB K Seavey
Dec 1, 1981·The Journal of Histochemistry and Cytochemistry : Official Journal of the Histochemistry Society·P OrdronneauP Petrusz

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Citations

Aug 30, 1996·Molecular and Cellular Endocrinology·A M NagyS Meuris

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