High affinity binding of ( super(125)I)monoiodoapamin to isolated guinea-pig hepatocytes

The bee venom neurotoxin apamin has been labelled with super(125)I and its binding to isolated guinea-pig hepatocytes measured under physiological conditions. A single saturable component of ( super(125)I)monoiodoapamin binding with a Kd of 350 pM and B sub(max) of 0.99 fmol/mg dry wt was identified...

Full description

Saved in:
Bibliographic Details
Published inFEBS letters Vol. 152; no. 2; pp. 263 - 269
Main Authors Cook, N S, Haylett, D G, Strong, P N
Format Journal Article
LanguageEnglish
Published 01.01.1983
Subjects
apamin
apis
Apoidea
guinea-pigs
hepatocytes
potassium
venom
Online AccessGet full text

Cover

More Information
Summary:The bee venom neurotoxin apamin has been labelled with super(125)I and its binding to isolated guinea-pig hepatocytes measured under physiological conditions. A single saturable component of ( super(125)I)monoiodoapamin binding with a Kd of 350 pM and B sub(max) of 0.99 fmol/mg dry wt was identified. Native apamin displaced labelled apamin with a K sub(d) 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 tissue, suggest that specific binding of labelled apamin is particularly associated with apamin-sensitive, Ca-activated K-channels.
Bibliography:ObjectType-Article-2
SourceType-Scholarly Journals-1
content type line 23
ObjectType-Feature-1
ISSN:0014-5793