Results 131 to 140 of about 20,141 (153)
Protein Expression and Purification, 2014 Sticholysin I and Sticholysin II (StI and StII) are two potent hemolysins which form pores in natural and model membranes at nanomolar concentrations.
Alberto del Monte-Martínez +9 more
semanticscholar +2 more sources
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Toxicon, 1988 A basic protein cytolysin previously isolated from the Caribbean sea anemone Stichodactyla helianthus was shown by CM cellulose chromatography to consist of four isotoxins possessing different N-terminal amino acid sequences. These are designated as toxins I-IV in order of increasing isoelectric point.
W. Kem, B. Dunn
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Pharmacological effects of two cytolysins isolated from the sea anemone Stichodactyla helianthus
Journal of Biosciences, 2009 Sticholysins I and II (St I/II) are cytolysins purified from the sea anemone Stichodactyla helianthus. In this study, we show their pharmacological action on guinea-pig and snail models in native and pH-denatured conditions in order to correlate the pharmacological findings with the pore-forming activity of both isoforms.
T. Garcia +8 more
semanticscholar +3 more sources
Toxicon, 2009 Sticholysin II (St II) is a toxin from the sea anemona Stichodactyla helianthus that produces erythrocytes lysis at low concentration and its activity depends on the presence of calcium. Calcium may act modifying toxin interaction with erythrocyte membranes or activating cellular processes which may result in a modified St II lytic action.
G. Celedón +9 more
semanticscholar +5 more sources
Biochemistry, 2016
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.
S. García-Linares +5 more
semanticscholar +3 more sources
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.
S. García-Linares +5 more
semanticscholar +3 more sources
Toxicon, 1989 The ability of a purified sea anemone (Stichodactyla helianthus) protein cytolysin to interact with a variety of interfaces was investigated by means of the Wilhemy plate method. At the air:water and lipid:water interfaces, the toxin lowered the surface pressure most readily as the aqueous phase pH increased towards the isoelectric point (9.8) of the ...
J. Doyle, W. Kem, F. Vilallonga
semanticscholar +4 more sources
Journal of Membrane Biology, 2001
The radius of the pore formed by sticholysin I and II (StI, StII) in erythrocytes and sticholysin I in lipid vesicles was investigated. The rate of colloid osmotic lysis of human erythrocytes, exposed to one of the toxins in the presence of sugars of different size, was measured.
M. Tejuca +4 more
semanticscholar +5 more sources
The radius of the pore formed by sticholysin I and II (StI, StII) in erythrocytes and sticholysin I in lipid vesicles was investigated. The rate of colloid osmotic lysis of human erythrocytes, exposed to one of the toxins in the presence of sugars of different size, was measured.
M. Tejuca +4 more
semanticscholar +5 more sources