Abstract
The amino acid sequence was determined for toxin F, a component of Bungarus multicinctus venom that blocks nicotinic transmission in the chick ciliary ganglion and the rat superior cervical ganglion. Toxin F was purified by a procedure that includes preparative isoelectric focusing and ion exchange chromatography. Seventy nanomolar toxin F blocks nicotinic transmission in the chick ciliary ganglion; however, the toxin only weakly blocks the binding of 125I-α-bungarotoxin to membranes derived from Torpedo californica electroplax (IC 50 = 1 μM). These data raise the possibility that toxin F may preferentially recognize neuronal nicotinic receptors. Toxin F focused identically on an isoelectric focusing gel with samples of two similar toxins, bungarotoxin 3.1 and χ-bungarotoxin. The sequence of toxin F is identical with that recently reported for χ-bungarotoxin. When the N-terminal portion of bungarotoxin 3.1 was sequenced, it was found to be identical to the other two toxins. These and other data suggest that the 3 toxins are, in fact, the same.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
