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Isolation and characterization of two opioid peptides from a bovine hemoglobin peptic hydrolysate.

Authors :
Piot JM
Zhao Q
Guillochon D
Ricart G
Thomas D
Source :
Biochemical and biophysical research communications [Biochem Biophys Res Commun] 1992 Nov 30; Vol. 189 (1), pp. 101-10.
Publication Year :
1992

Abstract

Two opioid peptides were isolated from a bovine hemoglobin hydrolysate, by use of gel permeation (GP) and reverse phase (RP) high performance liquid chromatography (HPLC). Their primary structure and accurate molecular weights, determined by amino acid analysis and fast atom bombardment (FAB) mass spectrometry, were identical to fragments 31-40 (LVV-hemorphin-7) and 32-40 (VV-hemorphin 7) of the beta-chain of bovine hemoglobin. The same fragments occur in human hemoglobin in positions 32-41 and 33-41 of the beta-chain, respectively. The opioid potency of these peptides, exhibited by use of electrically stimulated muscle of isolated guinea-pig ileum (GPI), were significant and comparable with some others previously described. In addition, the location of the two opioid peptides, VV-hemorphin-7 and LVV-hemorphin-7, revealed the existence of a "strategic zone" both in the bovine and human beta-chains of hemoglobin.

Details

Language :
English
ISSN :
0006-291X
Volume :
189
Issue :
1
Database :
MEDLINE
Journal :
Biochemical and biophysical research communications
Publication Type :
Academic Journal
Accession number :
1449465
Full Text :
https://doi.org/10.1016/0006-291x(92)91531-t