Action of neutral metalloendopeptidase ("enkephalinase") on β-endorphin

L. Gráf, A. Páldi, A. Patthy

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Human β-endorphin was digested by neutral metalloendopeptidase from rabbit kidney and the products were isolated and identified. Based on the structure and yield of the fragments, the major cleavage sites were identified with the Leu17-Phe18, Gly3-Phe4, Pro13-Leu14 and Ile22-Ile23 peptide bonds of the β-endorphin structure. The cleavage of the Leu17-Phe18 bond appears to be the rate-limiting step of the enzymic conversion similarly to the previously proposed pathways of β-endorphin degradation by brain homogenates and synaptic membranes.

Original languageEnglish
Pages (from-to)13-19
Number of pages7
JournalNeuropeptides
Volume6
Issue number1
DOIs
Publication statusPublished - 1985

Fingerprint

Metalloendopeptidases
Endorphins
Neprilysin
Synaptic Membranes
Brain
Rabbits
Membranes
Kidney
Degradation
Peptides

ASJC Scopus subject areas

  • Biochemistry
  • Endocrinology
  • Endocrinology, Diabetes and Metabolism
  • Clinical Neurology
  • Neuroscience(all)
  • Cellular and Molecular Neuroscience

Cite this

Action of neutral metalloendopeptidase ("enkephalinase") on β-endorphin. / Gráf, L.; Páldi, A.; Patthy, A.

In: Neuropeptides, Vol. 6, No. 1, 1985, p. 13-19.

Research output: Contribution to journalArticle

Gráf, L. ; Páldi, A. ; Patthy, A. / Action of neutral metalloendopeptidase ("enkephalinase") on β-endorphin. In: Neuropeptides. 1985 ; Vol. 6, No. 1. pp. 13-19.
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