{'fraction_non_alphanumeric': 0.03599374021909233, 'fraction_numerical': 0.04381846635367762, 'mean_word_length': 4.871559633027523, '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}}
Cloning and expression of the chicken CD18 cDNA

The leukocyte integrins play a critical role in a number of cellular adhesive interactions during the immune response. We describe here the isolation and characterization of the chicken β2 (CD18) subunit, common to the leukocyte integrin family. The deduced 748‐amino‐acid sequence reveals a transmembrane protein with 65% and 64% identity with its human and murine homo‐logues, respectively. The chicken β2 can associate on the cell surface with the human α subunit of LFA‐1 and yields a hybrid molecule capable of binding to purified ICAM‐1 and ICAM‐3. J. Leukoc. Biol. 55: 501–506; 1994.