The hemolytic effect of Salmonella typhi Ty 2 porins

Inés CALDERON, Sergio R. LOBOS, Guido C. MORA

Resultado de la investigación: Article

10 Citas (Scopus)

Resumen

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.

Idioma originalEnglish
Páginas (desde-hasta)579-583
Número de páginas5
PublicaciónEuropean Journal of Biochemistry
Volumen141
N.º3
DOI
EstadoPublished - 1984

Huella dactilar

Porins
Salmonella typhi
Salmonella
Heating
Agglomeration
Phenylglyoxal
Salmonella typhimurium
Hemolysis
Electrophoresis
Bacterial Infections
Sodium Dodecyl Sulfate
Detergents
Solubility
Purification
Gel Chromatography
Arginine
Polyacrylamide Gel Electrophoresis
Suspensions
Membrane Proteins
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

Citar esto

CALDERON, Inés ; LOBOS, Sergio R. ; MORA, Guido C. / The hemolytic effect of Salmonella typhi Ty 2 porins. En: European Journal of Biochemistry. 1984 ; Vol. 141, N.º 3. pp. 579-583.
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The hemolytic effect of Salmonella typhi Ty 2 porins. / CALDERON, Inés; LOBOS, Sergio R.; MORA, Guido C.

En: European Journal of Biochemistry, Vol. 141, N.º 3, 1984, p. 579-583.

Resultado de la investigación: Article

TY - JOUR

T1 - The hemolytic effect of Salmonella typhi Ty 2 porins

AU - CALDERON, Inés

AU - LOBOS, Sergio R.

AU - MORA, Guido C.

PY - 1984

Y1 - 1984

N2 - 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.

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