{'fraction_non_alphanumeric': 0.011627906976744186, 'fraction_numerical': 0.004651162790697674, 'mean_word_length': 4.979166666666667, '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}}
[Comparative study of the activity of arginase isoenzymes in brain tumors of humans and experimental animals].

Isoenzyme spectrum and total activity of arginase were studied in rat brain during growth of transplanted neurinoma and glioma as well as in malignant tissues of human brain. After transplantation of the tumors two peaks of arginase activation were observed within 2-4 days in rat brain tissues and within 16 days in tumoral tissue. Positively charged isoenzyme I of arginase was mainly activated but activity of neutral isoenzyme II was unaltered or slightly decreased. In human brain tumors activity of isoenzyme I was also prevailed, while activity of isoenzyme II was increased in some cases. Regulation of the arginase activity appears to occur by a complex mechanism and the enzyme plays a key role in development of nervous tissue neoplasms.