[T-proteins of Streptococcus pyogenes. III. Communication: purification of T-proteins extracted with trypsin, pepsin and C-phage-associated lysin by means of immunochromatography (author's transl)].
T-proteins of Streptococcus pyogenes type 1 were extracted by enzymatic treatment of cells with trypsin, pepsin or C-phage-associated lysin and subsequently purified by ion exchange chromatography on DEAE cellulose as well as by immuno-adsorption on immobilized anti-T-type 1 antibodies. Immunochromatographical purified T1-proteins which were extracted by the different enzymes showed different properties in immuno-electrophoresis, SDS-electrophoresis and amino acid composition although a serological reaction of identity was found in Ouchterlony precipitation. Tryptic and peptic digestion was efficient for extraction of T protein while the extraction with C-phage-associated lysin was unsuitable for isolation of T-protein. The release of T-protein after treatment of cells with this lysin was very low and the preparation purified by this way exhibited cross-reaction with non-absorbed antisera of other types.
D001426:Bacterial Proteins / Q000032:analysis / Q000276:immunology / Q000302:isolation & purification*; D004798:Enzymes; D000939:Epitopes; D005779:Immunodiffusion; D007163:Immunosorbent Techniques; D010434:Pepsin A; D013297:Streptococcus pyogenes / Q000032:analysis*; D014357:Trypsin
D001426:Bacterial Proteins; D004798:Enzymes; D000939:Epitopes; C028806:lysin, streptococcus bacteriophage; D014357:Trypsin; D010434:Pepsin A
T-Proteine des Streptococcus pyogenes. III. Mitteilung: Immunchromatographische Reinigung von T-Proteinen nach Extraktion mit Trypsin, Pepsin und C-phagen-assoziiertem Lysin.