{'fraction_non_alphanumeric': 0.04180064308681672, 'fraction_numerical': 0.02572347266881029, 'mean_word_length': 4.5625, '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}}
[An increase in the rate of proteolysis in vitro after treatment with oxidized glutathione].

The effect of the formation of mixed disulphides--protein-glutathione--on the proteolysis rate was studied using soluble fractions of proteins from different rat tissues as substrates. It was shown that the binding of oxidized glutathione to proteins increases the proteolysis rate under the effect of trypsin and chymotrypsin. When the concentration of oxidized glutathione is 5.10(-4) M a 1.2-1.4-fold increase in the proteolysis rate is registered and when the concentration is 5.10(-3) M a 1.4-1.8 fold increase is observed.