Ruder Bosković Institute, Department of Experimental Biology and Medicine, Zagreb, Croatia, Yugoslavia.
European journal of pharmacology 1991 Sep 4The binding of t-[3H]butylbicycloorthobenzoate ([3H]TBOB) to crude synaptosomal membranes of the mouse brain (cerebrum minus cortex) in the presence of dihydroergotoxine, dihydroergosine, dihydroergotamine and gamma-aminobutyric acid (GABA) was studied in vitro. [3H]TBOB binding was inhibited by all drugs used. The rank order of potency was dihydroergotoxine greater than GABA greater than dihydroergosine greater than dihydroergotamine. This suggests that dihydrogenated ergot compounds, especially dihydroergotoxine, possess appreciable binding activity (comparable to that of benzodiazepines and barbiturates) at the GABAA receptor-associated C1- ionophore.
A Tvrdeić, D Pericić. Dihydrogenated ergot compounds bind with high affinity to GABAA receptor-associated Cl- ionophore. European journal of pharmacology. 1991 Sep 4;202(1):109-11
PMID: 1664802
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