Abstract
The β-adrenergic antagonist propranolol was activated through its side chain, coupled to bovine serum albumin, and injected into BALB/c mice. After fusion of the splenocytes from these immunized mice with the NS-1 myeloma cell line, two hybridomas, producing monoclonal anti-propranolol antibodies, were isolated. Clone P-49 was monospecific for propranolol, with a significant preference for the 1-stereoisomer, as compared to the d form. On the other hand, clone P-28 cross-reacted with alprenolol as well as some other β-antagonists. Both classes of antibodies competed with A431 epidermoid carcinoma β2-adrenoceptors for the binding of [3H]propranolol. When ascites cells from clone P-28 were fixed with glutaraldehyde, the anti-propranolol monoclonal antibody became cell bound. These cell-bound P-28 antibodies bind propranolol and other β-adrenergic ligands with a similar ranking order to the soluble monoclonal antibody. The cell-bound antibody displayed a 5-fold higher affinity towards 1-propranolol than the soluble monoclonal antibody. The practical implications of these findings are discussed.
| Original language | English |
|---|---|
| Pages (from-to) | 173-178 |
| Number of pages | 6 |
| Journal | FEBS Letters |
| Volume | 199 |
| Issue number | 2 |
| DOIs | |
| State | Published - 21 Apr 1986 |
UN SDGs
This output contributes to the following UN Sustainable Development Goals (SDGs)
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SDG 3 Good Health and Well-being
Keywords
- Monoclonal antibody
- Propranolol
- Stereospecificity
- β-Adrenergic antagonist
- β-Adrenergic receptor
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