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Authordc.contributor.authorCalderón, Inés 
Authordc.contributor.authorLobos, S. es_CL
Authordc.contributor.authorMora, Guido C. es_CL
Admission datedc.date.accessioned2010-11-15T13:34:05Z
Available datedc.date.available2010-11-15T13:34:05Z
Publication datedc.date.issued1984
Cita de ítemdc.identifier.citationEuropean Journal of Biochemistry 141: 579-583en_US
Identifierdc.identifier.issn0014-2956
Identifierdc.identifier.urihttps://repositorio.uchile.cl/handle/2250/121115
Abstractdc.description.abstractTwo outer membrane proteins of Salmonella typhi T y 2 were extensively co-purified. According to their migration in dodecyl sulfate/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 T y 2. A critical step in the purification of porins is haeting at 100ºC in 2% sodium dodecyl sulfate before Sephadex gel filtration. The absence of detergent in aqueous suspensions enhances porin agregation, this aggregations inducing human red cell lysis. Porins obtained by an alternative procedure consisting of heating at 60ªC instead of 100ºC were also hemolytic. Using a 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.en_US
Lenguagedc.language.isoenen_US
Publisherdc.publisherSpringer-Verlagen_US
Keywordsdc.subjectSDSen_US
Títulodc.titleThe hemolytic effect of Salmonella typhi T y 2 porinsen_US
Document typedc.typeArtículo de revista


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