A simple biochemical method in the search for bioactive polypeptides in a sea anemone (Anemonia sulcata).
The sea anemone Anemonia sulcata is a well-known natural source of supply of biologically active polypeptides. So far, five toxins, ATX I, II, III, IV and AS V, several polyvalent protease inhibitors, an elastase inhibitor, two blood pressure-depressive polypeptides and very recently peptides that inhibit competitively the binding of 125I-dendrotoxin to rat brain membranes and block the voltage-sensitive K+ channels, have been isolated from it. The sea anemone toxins (especially toxin II of A. sulcata, ATX II) are very important tools in neurophysiological and pharmacological research, and their structure-function relationship has been investigated. Because of the great scientific value of the sea anemone toxins a simplification of their purification procedure was elaborated.
Sanchez
J
J
Institut für Toxikologie, Klinikum der Christian-Albrechts-Universität zu Kiel, Germany.
Bruhn
T
T
Aneiros
A
A
Wachter
E
E
Béress
L
L
D000818:Animals; D002850:Chromatography, Gel; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D003064:Cnidarian Venoms / Q000302:isolation & purification*; D010455:Peptides / Q000032:analysis / Q000302:isolation & purification*; D012615:Sea Anemones / Q000737:chemistry*
D003064:Cnidarian Venoms; D010455:Peptides