{'fraction_non_alphanumeric': 0.014925373134328358, 'fraction_numerical': 0.0, 'mean_word_length': 5.434343434343434, '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 cortactin by anion exchange chromatography

Cortactin is a cytoskeletal actin‐binding protein that is upregulated in several types of metastatic cancers. Standard purification of cortactin from E. coli involves expression of the protein as a His‐tagged protein followed by affinity purification with nickel resin. This purification is sometimes followed by anion exchange chromatography, which appears to result in a cortactin protein with enhanced activity in actin polymerization assays compared to cortactin that is only affinity purified. To determine how further purification by anion exchange chromatography alters the activity of the protein, we analyzed KCl elution fractions of cortactin on native polyacrylamide gels and found each elution fraction contained a different band pattern. These differences suggest that purification by anion exchange separates proteins of unique structures due to folding or modification of the protein. Future work includes biochemical analysis of the structure and modifications of cortactin in the elution fractions. This work was supported by an M.J. Murdock Charitable Trust Faculty Start Up Grant to A.E. Kruchten and a Linfield College Faculty Student Collaborative Research Award to A.E. Kruchten and K. Arns.