Degradation of luteinizing hormone-Releasing hormone (LHRH) by brain prolyl endopeptidase with release of des-glycinamide LHRH and glycinamide

S. Wilk, M. Benuck, M. Orlowski, N. Marks

Research output: Contribution to journalArticlepeer-review

27 Scopus citations

Abstract

A highly purified preparation of rabbit brain prolyl endopeptidase cleaved the decapeptide luteinizing hormone-releasing hormone (LHRH) at the Pro-Gly · NH2 bond leading to the release within 1-3 h incubation at 37°C of des-glycinamide LHRH and glycinamide. Evidence for this site of cleavage was obtained by the detection of glycinamide or glycine end groups by a microdanyslation procedure, and by separation of the breakdown products by high performance liquid chromatography (HPLC) on a reverse phase C-18 column. Incubation led to the appearance of two new peaks as detected by HPLC one of which was collected and shown to have the composition consistent with des-glycinamide LHRH. The other peak ran in the position identical to that of authentic glycinamide. Results suggest that prolyl endopeptidase could play a role in the inactivation of LHRH in vivo.

Original languageEnglish
Pages (from-to)275-279
Number of pages5
JournalNeuroscience Letters
Volume14
Issue number2-3
DOIs
StatePublished - Oct 1979
Externally publishedYes

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