Studies on the enzymic degradation of luteinizing hormone releasing hormone by rat pituitary plasma membranes

S. Elkabes, M. Fridkin, Y. Koch

Research output: Contribution to journalArticle

21 Scopus citations

Abstract

Degradation of luteinizing hormone releasing hormone (LH-RH) by purified plasma membranes from rat pituitaries was investigated. Synthetic LH-RH (0.5 mg/ml) was incubated (20 min, 37°C) with pituitary plasma membranes (750 μg protein/ml). The reaction was stopped by centrifugation at 4°C. The degradation products were isolated by high pressure liquid chromatography using a reversed-phase column. Amino acid analysis of the degradation products indicated that the N-terminal tripeptide (pGlu-His-Trp) and the N-terminal hexapeptide (pGlu-His-Trp-Ser-Tyr-Gly) sequence of LH-RH are the main degradation products. These results suggest that the main cleavage sites of LH-RH by the pituitary plasma membrane-bound enzymes are the Gly6-Leu7 and the Trp3-Ser4 bonds of the neurohormone.

Original languageEnglish (US)
Pages (from-to)240-248
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume103
Issue number1
DOIs
StatePublished - Nov 16 1981
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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