Results 101 to 110 of about 461 (139)
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Inmunolocalización de citolisinas en la anémona de mar (Stichodactyla helianthus)
2010Las sticholisinas I y II son dos proteínas citolíticas provenientes de la anémona de mar (Stichodactyla helianthus) que presentan un gran potencial biomédico. La ubicación de estas citolisinas dentro del tejido del animal sería un elemento de gran utilidad en el estudio de las funciones para las cuales este las emplea y facilitaría el proceso de ...
Ojito Ramos, Katia +1 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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European Journal of Biochemistry, 1993
The solution structure of a 55‐amino‐acid Kunitz‐type proteinase inhibitor, ShPI, purified from the Caribbean sea anemone Stichodactyla helianthus, was determined by NMR spectroscopy. Nearly complete sequence‐specific 1H‐NMR assignments were obtained at pH 4.6 and 36°C, and stereospecific assignments were determined for 23 pairs of diastereotopic ...
W, Antuch +4 more
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The solution structure of a 55‐amino‐acid Kunitz‐type proteinase inhibitor, ShPI, purified from the Caribbean sea anemone Stichodactyla helianthus, was determined by NMR spectroscopy. Nearly complete sequence‐specific 1H‐NMR assignments were obtained at pH 4.6 and 36°C, and stereospecific assignments were determined for 23 pairs of diastereotopic ...
W, Antuch +4 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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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 +8 more
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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 +8 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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Biochemistry, 1989
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.
R S, Norton, A I, Cossins, W R, Kem
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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.
R S, Norton, A I, Cossins, W R, Kem
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Biochemistry, 2003
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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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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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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