Use of Surface Plasmon Resonance to characterise binding of Botulinum Type A toxin-haemagglutinin complex to gangliosides Online publication date: Wed, 25-Jun-2008
by M.C. Blome, B.C. Yowler, R. O'Keeffe, N. Panjwani, A.M. Pickett, C-L. Schengrund
The Botulinum J. (TBJ), Vol. 1, No. 1, 2008
Abstract: Botulinum Type A toxin (BoNT/A)-haemagglutinin complex, marketed as Dysport®, is licensed for several clinical applications. Currently, potency is measured using the mouse lethality assay. To identify why preparations may differ, both endoprotease activity plus ability of the toxin complex to adhere to cells and be transported to where it acts must be monitored. Inhibition of any of those steps could affect efficacy. As a first step in such assessments, affinity of 9 different preparations of BoNT/A-haemagglutinin complex for ganglioside GT1b was measured using surface plasmon resonance. Similar binding affinities were obtained for all nine. [Received 4 October 2007; Accepted 12 November 2007]
Online publication date: Wed, 25-Jun-2008
If you are not a subscriber and you just want to read the full contents of this article, buy online access here.Complimentary Subscribers, Editors or Members of the Editorial Board of the The Botulinum J. (TBJ):
Login with your Inderscience username and password:
Want to subscribe?
A subscription gives you complete access to all articles in the current issue, as well as to all articles in the previous three years (where applicable). See our Orders page to subscribe.
If you still need assistance, please email firstname.lastname@example.org