IMIS

Publications | Institutes | Persons | Datasets | Projects | Maps
[ report an error in this record ]basket (0): add | show Print this page

Characterisation of neurotoxic polypeptides from Cyanea capillata medusae (Scyphozoa)
Lassen, S.; Helmholz, H.; Ruhnau, C.; Prange, A. (2010). Characterisation of neurotoxic polypeptides from Cyanea capillata medusae (Scyphozoa), in: Purcell, J.E. et al. Jellyfish blooms: New problems and solutions. Developments in Hydrobiology, 212: pp. 213-221. https://dx.doi.org/10.1007/978-90-481-9541-1_17
In: Purcell, J.E.; Angel, D.L. (Ed.) (2010). Jellyfish blooms: New problems and solutions. Developments in Hydrobiology, 212. Springer: Dordrecht. ISBN 978-90-481-9540-4; e-ISBN 978-90-481-9541-1. 234 pp. https://dx.doi.org/10.1007/978-90-481-9541-1, more
In: Dumont, H.J. (Ed.) Developments in Hydrobiology. Kluwer Academic/Springer: The Hague; London; Boston; Dordrecht. ISSN 0167-8418, more
Related to:
Lassen, S.; Helmholz, H.; Ruhnau, C.; Prange, A. (2010). Characterisation of neurotoxic polypeptides from Cyanea capillata medusae (Scyphozoa). Hydrobiologia 645(1): 213-221. https://dx.doi.org/10.1007/s10750-010-0215-x, more

Available in  Authors 

Keyword
    Marine/Coastal

Authors  Top 
  • Lassen, S.
  • Helmholz, H.
  • Ruhnau, C.
  • Prange, A.

Abstract
    Cnidarian venoms include neurotoxins, which are able to paralyse prey organisms immediately. Important targets for neurotoxins are voltage-gated ion channels in membranes of excitable cells. By blocking specific receptor sites, neurotoxic components disturb the physiological ion channel functions. Here, we describe the isolation and characterisation of potential neurotoxic polypeptides from the crude tentacle venom of the boreal scyphomedusan Cyanea capillata. Partially purified venom fractions were obtained by size-exclusion and subsequent reversed-phase chromatography. To assess the blocking activity of the venom on voltage-gated sodium channels, we modified a mouse neuroblastoma (MNB) cell assay. Venom fractions containing channel-blocking activity were analysed by matrix-assisted laser desorption ionisation time-of-flight mass spectrometry (MALDI-TOF MS). The resulting mass spectra revealed a cluster of singly charged peptides within a mass range from 3,900 to 7,000 Da. A group of three potentially neurotoxic peptides with molecular masses of 3983.4, 5795.4 and 6962.1 Da could be tracked throughout the purification process. This investigation of the crude venom is part of a multidimensional assay-guided approach for the isolation and structural characterisation of toxic polypeptides in northern Scyphozoa.

All data in the Integrated Marine Information System (IMIS) is subject to the VLIZ privacy policy Top | Authors