Cestèle S, Borchani L, El Ayeb M, Rochat H
Laboratoire de Biochimie, Ingénierie des Proteines, UMR6560, Université de la Méditerrannée, CNRS, Faculté de Médecine Nord, Marseille, France.
FEBS Lett. 1997 Mar 17;405(1):77-80. doi: 10.1016/s0014-5793(97)00160-9.
The insect-specific Bothus occitanus tunetanus IT2 toxin is distinguishable from other scorpion toxins by its amino acid sequence and effects on sodium conductance. The present study reveals that Bot IT2 possesses in cockroach neuronal membranes a single class of high affinity (Kd = 0.3 +/- 0.1 nM) and low capacity (Bmax = 2.4 +/- 0.5 pmol/mg) binding sites. Competitive binding experiments with several known sodium channel neurotoxins reveal that the Bot IT2 binding site is in close proximity to the other toxins.
