Luteinizing hormone-releasing hormone (LH-RH) activity of some synthetic polypeptides. I. Fragments shorter than decapeptide

A. V. Schally, A. Arimura, W. H. Carter, T. W. Redding, R. Geiger, W. König, H. Wissman, G. Jaeger, J. Sandow, N. Yanaihara, C. Yanaihara, T. Hashimoto, M. Sakagami

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50 Scopus citations

Abstract

The luteinizing-releasing hormone (LH-RH) activity of II synthetic polypeptides, some of which were speculatively reported as having LH-RH activity, was assayed in vivo and in vitro against pure natural and synthetic LH-RH. In vivo tests showed that (pyro)Glu-Tyr-Arg-Trp-NH2 had only 1 part in 7800 of the activity of the LH-RH decapeptide. (Pyro) Glu-Val-Ser-NH2, (pyro)Glu-Ser-Val-NH2 and (pyro)Glu-Gln-Ala-NH2, were inactive in vivo in doses as high as 5 - 20 μg/rat. Synthetic (pyro)Glu-His-Pro-amide (thyrotropin-releasing hormone) and a synthetic decapeptide proposed as growth-hormone-releasing hormone showed no LH-RH activity in doses up to 100 μg. N-terminal tripeptide and tetrapeptide fragments of LH-RH as well as the C-terminal octapeptide of LH-RH were also inactive. The C-terminal nonapeptide had an extremely low LH-RH activity (about 1 part in 50,000). The structure-activity relationship of LH-RH has been briefly discussed.

Original languageEnglish (US)
Pages (from-to)366-375
Number of pages10
JournalBiochemical and biophysical research communications
Volume48
Issue number2
DOIs
StatePublished - Jul 25 1972
Externally publishedYes

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Schally, A. V., Arimura, A., Carter, W. H., Redding, T. W., Geiger, R., König, W., Wissman, H., Jaeger, G., Sandow, J., Yanaihara, N., Yanaihara, C., Hashimoto, T., & Sakagami, M. (1972). Luteinizing hormone-releasing hormone (LH-RH) activity of some synthetic polypeptides. I. Fragments shorter than decapeptide. Biochemical and biophysical research communications, 48(2), 366-375. https://doi.org/10.1016/S0006-291X(72)80060-3