{'fraction_non_alphanumeric': 0.028419182948490232, 'fraction_numerical': 0.012433392539964476, 'mean_word_length': 5.0, '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}}
Purification of Human Elastase 1

Summary Elastase was obtained from human pancreas by extraction with sodium acetate buffer, pH 4.5, fractionation with ammonium sulfate, and adsorption on powdered elastin. The enzyme was eluted from elastin with dilute acetic acid and precipitated with ammonium sulfate. An orcein–elastin substrate was used for assay of the enzymatic activity. Maximum activity occurred at pH 8.6 to 8.9. Proelastase was not present in the purified preparations, i.e., there was no enhancement of enzymatic activity upon treatment with trypsin.