VLIZ
VLAAMS INSTITUUT VOOR DE ZEE
MARIEN EN KUSTGEBONDEN ONDERZOEK & BELEID IN VLAANDEREN
   
© VLIZ © VLIZ © VLIZ © VLIZ © VLIZ
 
 
  English  Sitemap  Print
U bent hier: VLIZ > datacentrum
menu1 Over het VLIZ menu2 Infoloket menu3 Zeebibliotheek menu4 Cijfers&Beleid menu5 Faciliteiten menu6 Datacentrum
   
Datacentrum
  - IMIS: Integrated Marine Information System -
log in

Personen | Instituten | Publicaties | Projecten | Datasets | Kaarten
meld een fout in dit recordmandje (0): toevoegen | tonen Print-vriendelijke versie

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. (Ed.) (2010). Jellyfish blooms: New problems and solutions. Developments in Hydrobiology, 212: pp. 213-221
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. 234 pp., meer
In: Dumont, H.J. (Ed.) Developments in Hydrobiology. Kluwer Academic/Springer: Den Haag. ISSN 0167-8418, meer

Ook gepubliceerd als
  • Lassen, S.; Helmholz, H.; Ruhnau, C.; Prange, A. (2010). Characterisation of neurotoxic polypeptides from Cyanea capillata medusae (Scyphozoa) Hydrobiologia 645(1): 213-221, meer

Beschikbaar in Auteurs 

Trefwoord
    Marien

Auteurs  Top 

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.

 Top | Auteurs 
 

 

Vlaams Instituut voor de Zee
InnovOcean site
Wandelaarkaai 7
B-8400 OOSTENDE, België
Tel: +32 [0]59/34 21 30
Fax: +32 [0]59/34 21 31
Email: info@vliz.be
   

 

Vlaamse Gemeenschap Provincie West-Vlaanderen