{'fraction_non_alphanumeric': 0.02127659574468085, 'fraction_numerical': 0.022396416573348264, 'mean_word_length': 5.525547445255475, '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 mouse liver UDPglucuronosyltransferase.

The present study describes a method for the purification of hepatic microsomal UDPglucuronosyltransferase from two different strains of mice, by a combination of detergent solubilization, ion-exchange chromatography and affinity chromatography. Using this procedure up to 0.5 mg of UDPglucuronosyltransferase could be obtained from 30 g of mouse liver and this enzyme could be purified from as little as 10 g of mouse liver. The molecular weight of the apparently homogeneous preparation was 57 000 +/- 2 000 when determined by sodium dodecyl sulphate polyacrylamide gel electrophoresis. The purified transferase catalysed the glucuronidation of approx. 0.6 mumol 4-nitrophenol min-1. mg-1 protein. Immunochemical analysis of this preparation further indicates that UDPglucuronosyltransferase has been purified to apparent homogeneity.