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• W2095235616 startingPage "107" @default.
• W2095235616 abstract "alpha-Hemolysin (HlyA) is a protein toxin (107 kDa) secreted by some pathogenic strains of E. coli. Several studies suggested the relationship between HlyA and lipopolysaccharide (LPS). We have studied experimentally the role of LPS on the stability and function of this toxin. The HlyA conformation in both, LPS-free and LPS-bound forms was investigated by tryptophan fluorescence. Studies about HlyA thermal and chemical denaturation indicated that its stability increased in the presence of LPS. On the other hand, the presence of negative and polar residues on the LPS reduced the tendency of HlyA to self-aggregation, and they may be the reservoir of calcium, cation essential for the lytic action of this toxin on red blood cells. These results suggest that HlyA and LPS are combined mainly via hydrophobic force to form an active toxin which stability is favored by the LPS." @default.
• W2095235616 created "2016-06-24" @default.
• W2095235616 creator A5002292602 @default.
• W2095235616 creator A5014315181 @default.
• W2095235616 creator A5042337334 @default.
• W2095235616 date "2005-06-01" @default.
• W2095235616 modified "2023-10-15" @default.
• W2095235616 title "Role of lipopolysaccharide on the structure and function of α-hemolysin from Escherichia coli" @default.
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• W2095235616 doi "https://doi.org/10.1016/j.chemphyslip.2005.02.009" @default.
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