Sandbox WWC6
From Proteopedia
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'''Alpha-hemolysin''' [https://en.wikipedia.org/wiki/Hemolysin#.CE.B1-hemolysin] is a toxin secreted by Staphylococcus aureus as a pore-forming heptamer that binds to eukaryotic cell membranes. This protein belongs to a family of bacterial exotoxins[http://www.uniprot.org/uniprot/P09616]. The primary function of alpha-hemolysin is cytolytic, and is achieved by the release of cytosolic K<sup>+</sup> ions from the through the hydrophilic, transmembrane portion of the beta-barrel pore[http://www.sciencedirect.com/science/article/pii/S0041010101001532]. | '''Alpha-hemolysin''' [https://en.wikipedia.org/wiki/Hemolysin#.CE.B1-hemolysin] is a toxin secreted by Staphylococcus aureus as a pore-forming heptamer that binds to eukaryotic cell membranes. This protein belongs to a family of bacterial exotoxins[http://www.uniprot.org/uniprot/P09616]. The primary function of alpha-hemolysin is cytolytic, and is achieved by the release of cytosolic K<sup>+</sup> ions from the through the hydrophilic, transmembrane portion of the beta-barrel pore[http://www.sciencedirect.com/science/article/pii/S0041010101001532]. | ||
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Revision as of 16:20, 16 April 2016
Function
Alpha-hemolysin [1] is a toxin secreted by Staphylococcus aureus as a pore-forming heptamer that binds to eukaryotic cell membranes. This protein belongs to a family of bacterial exotoxins[2]. The primary function of alpha-hemolysin is cytolytic, and is achieved by the release of cytosolic K+ ions from the through the hydrophilic, transmembrane portion of the beta-barrel pore[3].
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