{'fraction_non_alphanumeric': 0.019637462235649546, 'fraction_numerical': 0.019637462235649546, 'mean_word_length': 5.08256880733945, '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 and characterization of ceruloplasmin receptors.

Membrane receptors for ceruloplasmin were isolated by affinity chromatography using CP bound to CNBr-activated Sepharose 4B. The receptor was obtained in the form of a single sharp peak which when collected, concentrated and run on SDS-PAGE provided a single band with a molecular weight of 35,000. Treatment with endoglycosidase F reduced this molecular weight by 3%. It is concluded that ceruloplasmin receptors in this cell system is a membrane protein containing 3% carbohydrate with a total molecular weight of 35,000. It is possible that this is a monomer of a higher molecular weight protein.