doi: 10.1016/0014-5793(83)80393-7.
High affinity binding of [125I]monoiodoapamin to isolated guinea-pig hepatocytes
- PMID: 6298001
- DOI: 10.1016/0014-5793(83)80393-7
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High affinity binding of [125I]monoiodoapamin to isolated guinea-pig hepatocytes
FEBS Lett.
.
Free article
Abstract
The bee venom neurotoxin apamin has been labelled with 125I and its binding to isolated guinea-pig hepatocytes measured under physiological conditions. A single saturable component of [125I]monoiodoapamin binding with a Kd of 350 pM and Bmax of 0.99 fmol/mg dry wt was identified. Native apamin displaced labelled apamin with a Kd of 376 pM which is broadly in keeping with the concentrations found to inhibit K loss from guinea-pig hepatocytes. These observations, together with the binding found in other tissues, suggest that specific binding of labelled apamin is particularly associated with apamin-sensitive, Ca-activated K-channels.
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