Two outer membrane proteins of Salmonella typhi Ty 2 were extensively co‐purified. According to their migration in dodecylsulfate/polyacrylamide gel electrophoresis and solubility characteristics, these proteins are homologous to the 35‐kDa and 36‐kDa porins found in Salmonella typhimurium. A porin homologous to the 34‐kDa one has not been found in S. typhi Ty 2. A critical step in the purification of porins is heating at 100 °C in 2% sodium dodecyl sulfate before Sephadex gel filtration. The absence of detergent in aqueous suspensions enhances porin aggregation, these aggregations inducing human red cell lysis. Porins obtained by an alternative procedure consisting of heating at 60 °C instead of 100 °C were also hemolytic. Using nanomolar concentration of porins a strong influence of temperature on the hemolytic effect was observed. Porin‐induced hemolysis was inhibited with anti‐porin serum, as well as by a treatment with phenylglyoxal, which reacts with the arginine residues of proteins. The membrane‐disrupting ability of porins aggregates might explain some pathogenic characteristics of gram‐negative bacterial infections.
|Number of pages||5|
|Journal||European Journal of Biochemistry|
|Publication status||Published - 1984|
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