{'fraction_non_alphanumeric': 0.015444015444015444, 'fraction_numerical': 0.010296010296010296, 'mean_word_length': 6.072727272727272, '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}}
Isolation and Partial Characterization of the Allergen in Mountain Cedar Pollen

A biologically active fraction from a crude extract of mountain cedar pollen has been purified and partially chemically characterized. An ammonium bicarbonate extract of commercial defatted pollen was fractionated by G‐100 Sephadex chromatography and the biologically active fraction was found to be homogeneous by polyacrylamide gel electrophoresis and N‐terminal amino acid sequence analysis. The biologically active component is a 50,000 dalton protein whose N‐terminal amino acid sequence is Asp—Asn—Pro—lle—Asp. These findings provide a further purified pollen allergen for immunologic studies and the first such purified allergen having clinical significance in a limited geographic region.