Opioid peptides derived from hemoglobin: hemorphins

Biopolymers. 1997;43(2):75-98. doi: 10.1002/(SICI)1097-0282(1997)43:2<75::AID-BIP2>3.0.CO;2-X.

Abstract

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.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Binding, Competitive
  • Endopeptidases / metabolism
  • Hemoglobins / chemistry*
  • Hemoglobins / isolation & purification
  • Hemoglobins / metabolism
  • Hemoglobins / pharmacology
  • Hydrolysis
  • Macrophages, Peritoneal / enzymology
  • Macrophages, Peritoneal / metabolism
  • Molecular Sequence Data
  • Narcotic Antagonists / metabolism
  • Narcotic Antagonists / pharmacology
  • Opioid Peptides / chemistry*
  • Opioid Peptides / isolation & purification
  • Opioid Peptides / metabolism
  • Opioid Peptides / pharmacology
  • Peptide Fragments / chemistry*
  • Peptide Fragments / isolation & purification
  • Peptide Fragments / metabolism
  • Peptide Fragments / pharmacology
  • Receptors, Opioid / metabolism
  • Spectrometry, Mass, Fast Atom Bombardment

Substances

  • Hemoglobins
  • Narcotic Antagonists
  • Opioid Peptides
  • Peptide Fragments
  • Receptors, Opioid
  • hemorphin 7
  • Endopeptidases