Abstract
Pore-forming cytolysins of 19 kDa from sea anemones present a remarkable cytolytic property. In the present work, a purified 19-kDa cytolysin was obtained from the sea anemone Heteractis magnifica. The purification steps involved ammonium sulfate precipitation and subsequently desalting by dialysis against 10 mM sodium phosphate buffer (pH 7.4), followed by anion exchange chromatography in DEAE-Sepharose® column (GE Healthcare, Sweden) and gel filtration chromatography using Sephadex® G-50 matrix (GE Healthcare, Sweden). The active fractions from the gel filtration chromatography were pooled and rechromatographed in the same column. The final active fraction showed a prominent protein band of molecular mass of 19 kDa when analyzed by SDS-PAGE.
Highlights
Pore-forming cytolysins of 19 kDa from sea anemones present a remarkable cytolytic property
A highly active 19-kDa pore-forming cytolysin has been isolated from the mucus secretion and body homogenate of the sea anemone Heteractis magnifica [13,14,15,16]
The dialyzed fractions were purified by anion exchange chromatography on Hi-Trap DEAESepharose® anion-exchange column (0.7 x 2.5cm) (GE Healthcare, Sweden) at a flow rate of 60 mL/hour [20]
Summary
Pore-forming cytolysins of 19 kDa from sea anemones present a remarkable cytolytic property. A number of toxins have so far been isolated from various species of sea anemones and are well characterized [1,2,3]. A highly active 19-kDa pore-forming cytolysin has been isolated from the mucus secretion and body homogenate of the sea anemone Heteractis magnifica [13,14,15,16]. Though a number of toxins have been identified from sea anemones so far, the purification of the native proteins still remains a challenge.
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