{'fraction_non_alphanumeric': 0.018633540372670808, 'fraction_numerical': 0.007453416149068323, 'mean_word_length': 5.06015037593985, '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}}
[Molecular forms of acid proteinases of the brain].

Molecular forms of cathepsin D bound with subcellular structures were studied in the grey matter of the large hemispheres. Free and bound forms of the enzymes exposed to solubilization with detergent triton X-100 were fractionated by passage through a Sephadex G-100 column. Gel chromatographic analysis demonstrated three peaks of acid proteinase activity. Different areas of solubilization curves of acid proteinases corresponded to different molecular forms of cathepsins. The initial S-shape areas of solubilization curve corresponded to the first high molecular weight peak of the enzyme activity in the grey matter, whereas the subsequent linear ones -- to the second peak; the activity of free forms of the enzyme corresponded to the third peak.