[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.