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. 1983 May;80(9):2794–2798. doi: 10.1073/pnas.80.9.2794

Characterization of a teleost gonadotropin-releasing hormone.

N Sherwood, L Eiden, M Brownstein, J Spiess, J Rivier, W Vale
PMCID: PMC393915  PMID: 6341999

Abstract

A peptide that is recognized by certain antibodies raised against mammalian gonadotropin-releasing hormone has been purified from extracts of salmon brains by gel filtration and high-performance liquid chromatography. The primary structure of this 10-residue peptide is less than Glu-His-Trp-Ser-Tyr-Gly-Trp-Leu-Pro-Gly-NH2. This represents a difference of two amino acids between salmon and mammalian gonadotropin-releasing hormone and demonstrates that most of the molecule has been conserved during evolution. The synthetic form of salmon gonadotropin-releasing hormone is less potent than is mammalian gonadotropin-releasing hormone on mammalian cells and is biologically active in salmon.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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