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The solution properties of the polypeptide neurotoxin I from the sea anemone Stichodactyla helianthus (Sh I) have been investigated by high-resolution 1H nuclear magnetic resonance (NMR) spectroscopy at 300 MHz. The pH dependence of the spectra has been examined over the range 1.1-12.2 at 27 degrees C.
Raymond S. Norton +2 more
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Biochemistry, 1989
An aqueous exudate collected from frozen and thawed bodies of a Caribbean sea anemone, Stichodactyla (formerly Stoichactis) helianthus, contained a polypeptide neurotoxin (Sh I) selectively toxic to crustaceans. The polypeptide was purified by G-50 Sephadex, phosphocellulose, and sulfopropyl-Sephadex chromatography and shown to have a molecular size of
W R, Kem +4 more
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An aqueous exudate collected from frozen and thawed bodies of a Caribbean sea anemone, Stichodactyla (formerly Stoichactis) helianthus, contained a polypeptide neurotoxin (Sh I) selectively toxic to crustaceans. The polypeptide was purified by G-50 Sephadex, phosphocellulose, and sulfopropyl-Sephadex chromatography and shown to have a molecular size of
W R, Kem +4 more
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Actinoporins are pore-forming toxins from sea anemones. Upon interaction with sphingomyelin-containing bilayers, they become integral oligomeric membrane structures that form a pore. Sticholysin II from Stichodactyla helianthus contains five tryptophans located at strategic positions; its role has now been studied using different mutants.
Sara García‐Linares +5 more
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Archives of medical research, 1994
A Kunitz type proteinase inhibitor was isolated from extracts of the sea anemone Stichodactyla helianthus. The purification procedure comprises treatment with trichloroacetic acid followed by affinity chromatography on trypsin-Sepharose and gel filtration on Sephadex G-50 or ion exchange chromatography on CM-cellulose.
J, Delfín +3 more
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A Kunitz type proteinase inhibitor was isolated from extracts of the sea anemone Stichodactyla helianthus. The purification procedure comprises treatment with trichloroacetic acid followed by affinity chromatography on trypsin-Sepharose and gel filtration on Sephadex G-50 or ion exchange chromatography on CM-cellulose.
J, Delfín +3 more
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ShK, a peptide isolated from Stichodactyla helianthus venom, blocks the voltage-gated potassium channels, K(v)1.1 and K(v)1.3, with similar high affinity. ShK-Dap(22), a synthetic derivative in which a diaminopropionic acid residue has been substituted at position Lys(22), has been reported to be a selective K(v)1.3 inhibitor and to block this channel ...
Richard E. Middleton +17 more
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Protein Expression and Purification, 2000
The cDNA coding for the cytolytic toxins sticholysin I and sticholysin II from the sea anemone Stichodactyla helianthus has been isolated, cloned in pUC18, and sequenced. A 6His-tagged version of sticholysin II has been overproduced in Escherichia coli and purified to homogeneity in milligram amounts.
V, de los Ríos +6 more
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The cDNA coding for the cytolytic toxins sticholysin I and sticholysin II from the sea anemone Stichodactyla helianthus has been isolated, cloned in pUC18, and sequenced. A 6His-tagged version of sticholysin II has been overproduced in Escherichia coli and purified to homogeneity in milligram amounts.
V, de los Ríos +6 more
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Toxicology in Vitro, 2007
The haemolytic and peroxidative effects of crude venom of the sea anemone Stichodactyla helianthus were evaluated in rat and human erythrocytes. Venom extract caused a significant concentration-dependent effect on haemolysis (release of haemoglobin). Human erythrocytes were more sensitive (0.094 mg protein/ml) than those of the rats (0.3787 mg protein ...
Heidi Irais, Monroy-Estrada +4 more
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The haemolytic and peroxidative effects of crude venom of the sea anemone Stichodactyla helianthus were evaluated in rat and human erythrocytes. Venom extract caused a significant concentration-dependent effect on haemolysis (release of haemoglobin). Human erythrocytes were more sensitive (0.094 mg protein/ml) than those of the rats (0.3787 mg protein ...
Heidi Irais, Monroy-Estrada +4 more
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Toxicon, 2003
Sticholysin II (St II) a potent cytolysin from the sea anemone Stichodactyla helianthus was obtained by recombinant procedures exhibiting six histidine residues in its N-terminus (St IIn6H). The functional comparison between St II and St IIn6H showed a lesser pore-forming ability for the recombinant than for the native in human or rat red blood cells ...
I F, Pazos +7 more
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Sticholysin II (St II) a potent cytolysin from the sea anemone Stichodactyla helianthus was obtained by recombinant procedures exhibiting six histidine residues in its N-terminus (St IIn6H). The functional comparison between St II and St IIn6H showed a lesser pore-forming ability for the recombinant than for the native in human or rat red blood cells ...
I F, Pazos +7 more
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Sticholysin I (St I) is a potent cytolytic polypeptide purified from the Caribbean sea anemone Stichodactyla helianthus. The hemolytic activity of sticholysin is potentiated by its preincubation at high ionic strengths. In the present work the mechanism of the potentiating action of the medium ionic strength on the toxin hemolytic capacity is ...
Carlos Álvarez +9 more
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Biochemistry, 1989
Sequence-specific assignments are reported for the 500-MHz 1H nuclear magnetic resonance (NMR) spectrum of the 48-residue polypeptide neurotoxin I from the sea anemone Stichodactyla helianthus (Sh I). Spin systems were first identified by using two-dimensional relayed or multiple quantum filtered correlation spectroscopy, double quantum spectroscopy ...
R H, Fogh +3 more
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Sequence-specific assignments are reported for the 500-MHz 1H nuclear magnetic resonance (NMR) spectrum of the 48-residue polypeptide neurotoxin I from the sea anemone Stichodactyla helianthus (Sh I). Spin systems were first identified by using two-dimensional relayed or multiple quantum filtered correlation spectroscopy, double quantum spectroscopy ...
R H, Fogh +3 more
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