Primary Structure of the Ovine Hypothalamic Luteinizing Hormone-releasing Factor (LRF) (LH-hypothalamus-LRF-gas Chromatography-mass Spectrometry-decapeptide-Edman Degradation)

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1972 Jan 1

PMID 4550508

Citations 69

Authors

R Burgus

M Butcher

M Amoss

N Ling

M Monahan

J Rivier

R Fellows

R Blackwell

W Vale

R Guillemin

Affiliations

Soon will be listed here.

Abstract

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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