Primary structure of the ovine hypothalamic luteinizing hormone-releasing factor (LRF) (LH-hypothalamus-LRF-gas chromatography-mass spectrometry-decapeptide-Edman degradation).

نویسندگان

  • R Burgus
  • M Butcher
  • M Amoss
  • N Ling
  • M Monahan
  • J Rivier
  • R Fellows
  • R Blackwell
  • W Vale
  • R Guillemin
چکیده

The primary structure of ovine hypothalamic hypophysiotropic luteinizing hormone-releasing factor, LRF, has been established as pGlu-His-Trp-Ser-Tyr-Gly-Leu-Arg-Pro-Gly-NH(2) by hydrolysis of the peptide with chymotrypsin or pyrrolidone-carboxylylpeptidase and by analysis of the products by an Edman-dansylation sequencing technique, as well as by mass spectrometry of the derived phenylthiohydantoins. A decapeptide with the proposed primary structure, prepared by total synthesis, gave the same result on sequencing. The synthetic decapeptide possesses the same biological activities as the native ovine LRF. The amino-acid sequence of ovine LRF is identical to that already published for porcine LRF.

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عنوان ژورنال:
  • Proceedings of the National Academy of Sciences of the United States of America

دوره 69 1  شماره 

صفحات  -

تاریخ انتشار 1972