Proceedings of the National Academy of Sciences · 1972 · 475 citations · 19 references
Life SciencesBiochemistryMolecular BiologyEnzymologyHormone BiochemistryNeuroendocrinologyHormone BiosynthesisHormone ReleaseHormone StructurePeptide Hormone BiochemistryProtein StructureProteolytic ProcessingAmino Acid Sequence-structure RelationshipsAmino Acid-derived Hormone StructureHormone Primary StructureHypothalamic-releasing HormonesPeptide Hormone StructurePeptide Mass SpectrometryProtein HormonesReleasing Hormones
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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