{'fraction_non_alphanumeric': 0.029074215761285386, 'fraction_numerical': 0.02218821729150727, 'mean_word_length': 4.662337662337662, 'pattern_counts': {'":': 0, '<': 0, '<?xml version=': 0, '>': 0, 'https://': 0, 'lorem ipsum': 0, 'www.': 0, 'xml': 0}, 'pii_count': 0, 'substrings_counts': 0, 'word_list_counts': {'cursed_substrings.json': 0, 'profanity_word_list.json': 0, 'sexual_word_list.json': 0, 'zh_pornsignals.json': 0}}
[T-proteins of Streptococcus pyogenes. I. Communication: Preparation of a serological type specific T1-antigen by ion exchange chromatography and its characterization (author's transl)].

The T-protein of Streptococcus pyogenes type 1 was trypsin-extracted and subsequently purified by ion exchange chromatography on CM and DEAE cellulose. Fractionation on CM cellulose by stepwise increase of the pH did not result in separation of type specific material from cross reacting components. The bulk of serologically active material was eluted at pH 5.6. On DEAE cellulose a type specific fraction was eluted with 0.05 m phosphate buffer, pH 8.2. A second fraction eluted with 0.25 m NaCl in the same buffer contained type specific as well as cross reacting material. Molecular weight distributions of type-specific T-protein were studied by gel chromatography on Ultrogel ACA44 and Biogel A 1.5 m. A multiple size subunit structure of T-protein was found and supported by SDS electrophoresis. Molecular weights of fragments serologically active in double diffusion were detected in a range of 37 000 to more than 200 000 Dalton. The isoelectric point was determined as to be pH 4.5. The purified T-protein was found to be free of cystein and of the amino sugars N-acetyl-glucosamine and N-acetyl-muramic acid.