A monoclonal antibody that inhibits opioid binding to rat brain membranes

S. Roy, Y. X. Zhu, H. H. Loh, N. M. Lee

Research output: Contribution to journalArticle

17 Scopus citations

Abstract

To understand the structure-function relationship and to probe the molecular characteristics of the purified opioid receptor, monoclonal antibodies (mab) were raised against a purified opioid receptor protein. After intensive screening of almost 1500 hybridoma cell lines, only 7 clones were shown to have very high immunoreactivity against the purified receptor. Moreover, out of these 7 clones, only 2, 3B4F11 and 3A27G, were found to inhibit the ligand binding property of the mu-opioid receptor. The mab 3B4F11 was found to inhibit 3H-diprenorphine binding to the purified receptor in a dose dependent manner with a maximal inhibition of 100% achieved with 20μg of the antibody. Likewise, Fab fragments prepared from the mabs 3B4F11 inhibited 3H-diprenorphine binding to P2 membranes in a dose-dependent manner. In addition, it was found that the binding of 3H-DAGO, 3H-DPDPE and 3H-EKC was inhibited with approximately equal potency, suggesting that the Fabs prepared from the mab 3B4F11 interact with all 3 receptor types.

Original languageEnglish (US)
Pages (from-to)688-693
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume154
Issue number2
DOIs
StatePublished - Jul 29 1988

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