Results 141 to 150 of about 20,141 (153)
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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
semanticscholar +3 more sources
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
semanticscholar +3 more sources
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 ...
R. Middleton +17 more
semanticscholar +3 more sources
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 ...
R. Middleton +17 more
semanticscholar +3 more sources
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
openaire +1 more source
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
openaire +2 more sources
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
openaire +2 more sources
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
openaire +1 more source
Journal of Experimental Zoology Part A Comparative Experimental Biology, 2006
Ariel Basulto +5 more
semanticscholar +1 more source
Ariel Basulto +5 more
semanticscholar +1 more source

