Toogood_1984_Neuropeptides_5_121

Reference

Title : [125I] Tyr27 beta-endorphin: a radio-iodinated derivative of beta-endorphin for the study of opiate receptors - Toogood_1984_Neuropeptides_5_121
Author(s) : Toogood CI , McFarthing KG , Hulme EC , Smyth DG
Ref : Neuropeptides , 5 :121 , 1984
Abstract :

Evidence is presented that a new derivative of beta-endorphin, [125I] Tyr27 beta-endorphin, is a suitable ligand for the study of beta-endorphin binding sites in rat brain. The results obtained with this homogeneous mono-iodinated peptide demonstrated high affinity agonist binding sensitive to the presence of sodium and magnesium ion and to guanine nucleotide. Competition experiments using a series of opiates and opioid peptides including shorter forms of beta-endorphin revealed a range of potencies; beta-endorphin 1-31 exhibited the highest affinity. The findings suggest that binding sites that complement the structure of beta-endorphin are present in rat cortex.

PubMedSearch : Toogood_1984_Neuropeptides_5_121
PubMedID: 6099478

Related information

Citations formats

Toogood CI, McFarthing KG, Hulme EC, Smyth DG (1984)
[125I] Tyr27 beta-endorphin: a radio-iodinated derivative of beta-endorphin for the study of opiate receptors
Neuropeptides 5 :121

Toogood CI, McFarthing KG, Hulme EC, Smyth DG (1984)
Neuropeptides 5 :121