VV-hemorphin-7 and LVV-hemorphin-7 released during in vitro peptic hemoglobin hydrolysis are morphinomimetic peptides.
Two opioid peptides were generated by in vitro pepsin treatment of bovine hemoglobin. These peptides were identified using a GPI test and purified using HPLC chromatographic techniques. They correspond to fragments 31-40 (LVV-hemorphin-7) and 32-40 (VV-hemorphin-7) of the beta-chain of bovine hemoglobin. Binding experiments strongly confirm that VV-hemorphin-7 and LVV-hemorphin-7 are opioid peptides since they inhibited [3H]naloxone binding to rat brain membranes. Our results indicate that VV-hemorphin-7 and LVV-hemorphin-7 exhibit a lesser potency both in GPI and binding tests. Selectivity and affinity of these purified peptides and synthetic hemorphin-7 for opioid receptors is discussed.
Garreau
I
I
Laboratoire de Génie Protéique et Cellulaire, Pôle Sciences et Techniques, La Rochelle, France.
Zhao
Q
Q
Pejoan
C
C
Cupo
A
A
Piot
J M
JM
D000818:Animals; D001667:Binding, Competitive; D002417:Cattle; D020875:Enkephalin, Ala(2)-MePhe(4)-Gly(5)-; D004743:Enkephalin, Leucine / Q000031:analogs & derivatives / Q000494:pharmacology; D004745:Enkephalins / Q000494:pharmacology; D006168:Guinea Pigs; D006454:Hemoglobins / Q000378:metabolism*; D006868:Hydrolysis; D007082:Ileum / Q000378:metabolism; D008297:Male; D009020:Morphine / Q000819:agonists*; D009270:Naloxone / Q000494:pharmacology; D010434:Pepsin A / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D011957:Receptors, Opioid / Q000819:agonists*; D012680:Sensitivity and Specificity
D004745:Enkephalins; D006454:Hemoglobins; D010446:Peptide Fragments; D011957:Receptors, Opioid; D020875:Enkephalin, Ala(2)-MePhe(4)-Gly(5)-; D009270:Naloxone; D004743:Enkephalin, Leucine; C034318:enkephalin, Ser(2), Leu(5), Thr(6)-; C074309:LVV-hemorphin-7; C094394:VV-hemorphin-7; D009020:Morphine; D010434:Pepsin A