Results 121 to 130 of about 20,141 (153)
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Toxicon, 2001
Sticholysin I (St-I) and sticholysin II (St-II) are cytolysins purified from the sea anemone Stichodactyla helianthus with a high degree of sequence identity (93%) but clearly differenced in their hemolytic activity. In order to go further into the structural determinants for the different behavior of St-I and St-II, we report here the complete amino ...
Vivian Morera +2 more
exaly +9 more sources
Sticholysin I (St-I) and sticholysin II (St-II) are cytolysins purified from the sea anemone Stichodactyla helianthus with a high degree of sequence identity (93%) but clearly differenced in their hemolytic activity. In order to go further into the structural determinants for the different behavior of St-I and St-II, we report here the complete amino ...
Vivian Morera +2 more
exaly +9 more sources
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
Michael W Pennington +2 more
exaly +4 more sources
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
Michael W Pennington +2 more
exaly +4 more sources
Toxicon, 2006 Sticholysins I and II (Sts I and II) are two potent cytolysins from the sea anemone Stichodactyla helianthus. These isoforms present 13 substitutions, with three non-conservative located at the N-terminus. St II is considerably more hemolytic than St I in human red blood cells, a result explained by the smaller number of negatively charged groups ...
F Pazos, Amaury Pupo, Mayra Tejuca
exaly +6 more sources
Toxicon, 1998
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 Alvarez +2 more
exaly +4 more sources
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 Alvarez +2 more
exaly +4 more sources
Protein Expression and Purification, 2016
The major protease inhibitor from the sea anemone Stichodactyla helianthus (ShPI-1) is a non-specific inhibitor that binds trypsin and other trypsin-like enzymes, as well as chymotrypsin, and human neutrophil elastase. We performed site-directed mutagenesis of ShPI-1 to produce two variants (rShPI-1/K13L and rShPI/Y15S) that were expressed in Pichia ...
Rossana García-Fernández +2 more
exaly +4 more sources
The major protease inhibitor from the sea anemone Stichodactyla helianthus (ShPI-1) is a non-specific inhibitor that binds trypsin and other trypsin-like enzymes, as well as chymotrypsin, and human neutrophil elastase. We performed site-directed mutagenesis of ShPI-1 to produce two variants (rShPI-1/K13L and rShPI/Y15S) that were expressed in Pichia ...
Rossana García-Fernández +2 more
exaly +4 more sources
Toxicon, 2002
Stichodactyla helianthus is a sea anemone relatively abundant along Cuban coasts appearing in two morphos with different colors in their tentacles: green or brownish, probably due to their association with algal symbionts. Traditionally, the brownish morpho has been used as a source of sticholysins I and II, the most characterized cytolysins from this ...
Vivian Morera +2 more
exaly +4 more sources
Stichodactyla helianthus is a sea anemone relatively abundant along Cuban coasts appearing in two morphos with different colors in their tentacles: green or brownish, probably due to their association with algal symbionts. Traditionally, the brownish morpho has been used as a source of sticholysins I and II, the most characterized cytolysins from this ...
Vivian Morera +2 more
exaly +4 more sources
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 ...
Mayra Tejuca +2 more
exaly +4 more sources
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 ...
Mayra Tejuca +2 more
exaly +4 more sources
Chemical synthesis of a neurotoxic polypeptide from the sea anemone Stichodactyla helianthus.
International Journal of Peptide and Protein Research, 2009 The sea anemoneStichodactyla helianthusneurotoxin I, a 48‐residue polypeptide, was synthesized by automated solid phase methodology. The fully reduced polypeptide was subsequently refolded in the presence of a glutathione oxidoreduction buffer to the biologically active species containing three disulfide bonds.
M. Pennington +3 more
semanticscholar +4 more sources
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 ...
Sonia Galván-Arzate +2 more
exaly +4 more sources
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 ...
Sonia Galván-Arzate +2 more
exaly +4 more sources
Toxicon, 1996
Isolation of proteinase inhibitors from the sea anemone Stichodactyla helianthus was achieved by trichloroacetic acid treatment of the aqueous extract followed by affinity chromatography on trypsin-Sepharose and ion-exchange chromatography on CM-cellulose. The average molecular mass of the major inhibitor (ShPI-I) obtained by fast atom bombardment mass
J. Delfín +11 more
semanticscholar +4 more sources
Isolation of proteinase inhibitors from the sea anemone Stichodactyla helianthus was achieved by trichloroacetic acid treatment of the aqueous extract followed by affinity chromatography on trypsin-Sepharose and ion-exchange chromatography on CM-cellulose. The average molecular mass of the major inhibitor (ShPI-I) obtained by fast atom bombardment mass
J. Delfín +11 more
semanticscholar +4 more sources