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Opioid peptides derived from hemoglobin: Hemorphins
Author(s) -
Zhao Q.,
Garreau I.,
Sannier F.,
Piot J. M.
Publication year - 1997
Publication title -
peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1997)43:2<75::aid-bip2>3.0.co;2-x
Subject(s) - chemistry , hydrolysate , hemoglobin , opioid peptide , peptide , globin , hydrolysis , derivative (finance) , amino acid , opioid , receptor , biochemistry , chromatography , pharmacology , medicine , financial economics , economics
Investigation of hemoglobin peptic hydrolysate has revealed the presence of biologically active peptides with affinity for opioid receptors. Two peptides, VV‐hemorphin‐7 and LVV‐hemorphin‐7, were resolved by a combination of size exclusion and reversed phase HPLC. A new spectroscopic method based on the second order derivative spectra analysis of aromatic amino acids has been developed. This method allows qualitative and quantitative evaluation of hemorphins generated by peptic hemoglobin hydrolysis. Using this method, a kinetic study of hemorphins appearance has been undertaken. In this paper, we also evidenced the generation of VV‐hemorphin‐7 from globin by peritoneal macrophages. In regard to this result, the putative physiological role of hemorphins is discussed. © 1997 John Wiley & Sons, Inc. Biopoly 43: 75–98, 1997