Purification and some properties of a lethal toxic fragment of staphylococcal α-toxin by tryptic digestion

摘要: Abstract Purified staphylococcal α-toxin (molecular weight approximately 36 000) was mildly digested with trypsin, yielding two components by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. A fast-moving component 17 000 ± 5%) which is relatively resistant to tryptic digestion and a slow-moving 20 tends aggregate. The highly purified means of combined procedures column chromatography on Sephadex G-200 zone electrophoresis starch. retained high degree lethal toxicity for mouse but lacked hemolytic dermonecrotic activities, whereas the proved be nontoxic polypeptide. toxic fragment antigenically active showing partial immunological identity parent stimulated formation antibodies capable neutralizing action in vivo. Some physical properties amino acid composition have been compared those native α-toxin.