Literature DB >> 2992491

Conversion and inactivation of opioid peptides by rabbit brain endo-oligopeptidase A.

A C Camargo, M J Ribeiro, W N Schwartz.   

Abstract

The conversion of BAM-12P to Met-enkephalin and the hydrolysis of the Phe-Met and Phe-Leu bonds of met-enkephalin-Arg-Phe and Leu-enkephalin-Arg-Arg, respectively, by rabbit brain endo-oligopeptidase A were demonstrated. Peptide fragments were isolated by high performance liquid chromatography and identified by amino acid analysis. BAM 22P was not hydrolysed by the enzyme. The concentration dependent inhibition of BAM-12P conversion into Met-enkephalin by bradykinin and vice-versa provided additional evidence that endo-oligopeptidase A cleaves both the Phe5-Ser6 bond in bradykinin and the Met5-Arg6 bond of BAM-12P.

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Year:  1985        PMID: 2992491     DOI: 10.1016/0006-291x(85)90506-6

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  3 in total

Review 1.  Proteolytic enzymes in the post-translational processing of polypeptide hormone precursors.

Authors:  P Gluschankof; P Cohen
Journal:  Neurochem Res       Date:  1987-10       Impact factor: 3.996

2.  Enkephalin is liberated from metorphamide and dynorphin A1-8 by endo-oligopeptidase A, but not by metalloendopeptidase EC 3.4.24.15.

Authors:  O Toffoletto; K M Metters; E B Oliveira; A C Camargo; J Rossier
Journal:  Biochem J       Date:  1988-05-15       Impact factor: 3.857

3.  Chicken liver Pz-peptidase, a thiol-dependent metallo-endopeptidase.

Authors:  A J Barrett; M A Brown
Journal:  Biochem J       Date:  1990-11-01       Impact factor: 3.857

  3 in total

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