RESUMO
Hydrophobic chromatography on phenyl-Sepharose has revealed the decidedly hydrophobic character of several members of the group of cytolytic proteins termed ;thiol-activated'. Pneumolysin, alveolysin, cereolysin, and streptolysin O were found to be equally hydrophobic, as were the oxidized and reduced forms of alveolysin. Hydrophobic chromatography has been utilized in the development of an improved procedure for the purification of pneumolysin.
Assuntos
Citotoxinas , Proteínas de Bactérias , Cromatografia de Afinidade , Sefarose/análogos & derivados , Estreptolisinas/isolamento & purificação , Compostos de SulfidrilaRESUMO
Pneumolysin-negative mutants of Streptococcus pneumoniae were isolated after mutagenesis with ethyl methane sulfonate. Though totally devoid of pneumolysin, these strains produced alpha hemolysis on blood agar when incubated aerobically. It is concluded that the alpha hemolysis typical of pneumococci is unrelated to their pneumolysin content.
