{'fraction_non_alphanumeric': 0.03928170594837262, 'fraction_numerical': 0.020202020202020204, 'mean_word_length': 5.371428571428571, '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}}
Human kininogen from Cohns Fraction IV: comparisons of antigenicity and multiple forms.

Kininogen was isolated from Cohns fraction IV by DEAE-chromatography, gel filtration and ammonium sulphate precipitation. Immunologically pure kininogen was prepared by removal of protein impurities using specific immunoadsorbents with Sepharose-bound antibody. Anti-kininogen serum was raised in rabbits against the pure antigen. Comparison with anti-kininogen sera prepared with the biologically active LMW antigen from whole plasma suggested antigenic identity by double immunodiffusion analysis. The Cohn-kininogen was shown to contain mainly two components (85%) in about equal amounts focusing with peaks at pI 4.2 (42%) and pI 4.3 (43%). These represent apparently structurally altered forms of the native plasma kininogen focusing at pI 4.5-4.6 (54%), which occurred as a minor component (13%).