Purified opioid mu-receptor is of a different molecular size than delta- and kappa-receptors

Neurosci Lett. 1987 Apr 10;75(3):339-44. doi: 10.1016/0304-3940(87)90546-5.

Abstract

Opioid mu-receptors were solubilized from rat brains with 0.5% Triton X-100 in the presence of 0.32 M sucrose and then purified with 6-succinyl morphine-Affi-Gel 102 column. Purified materials showed a major band with mol.wt. 58,000 Da and a minor band with mol.wt. 41,000 Da. Affinity cross linking with [3H]DAGO, a selective mu-opioid agonist, to the neural membranes and purified materials revealed that opioid mu-binding protein has a mol.wt. of 58,000 Da, a value totally different from that of delta- (mol.wt. 18,500 Da) and kappa- (mol.wt. 36,000 Da) binding protein.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Brain Chemistry*
  • Chemical Phenomena
  • Chemistry
  • Dynorphins / metabolism
  • Enkephalin, Ala(2)-MePhe(4)-Gly(5)-
  • Enkephalin, D-Penicillamine (2,5)-
  • Enkephalins / metabolism
  • Ligands
  • Male
  • Peptide Fragments / metabolism
  • Rats
  • Rats, Inbred Strains
  • Receptors, Opioid / isolation & purification*
  • Receptors, Opioid, delta
  • Receptors, Opioid, kappa
  • Receptors, Opioid, mu

Substances

  • Enkephalins
  • Ligands
  • Peptide Fragments
  • Receptors, Opioid
  • Receptors, Opioid, delta
  • Receptors, Opioid, kappa
  • Receptors, Opioid, mu
  • Enkephalin, Ala(2)-MePhe(4)-Gly(5)-
  • Dynorphins
  • Enkephalin, D-Penicillamine (2,5)-