{"id":{"repo_id":"uiuc","oai_identifier":"oai:www.ideals.illinois.edu:2142/86671"},"canonical_url":"https://search.dev.ndltd.org/etd/uiuc/oai:www.ideals.illinois.edu:2142/86671","repository":{"repo_id":"uiuc","name":"University of Illinois - Urbana-Champaign","base_url":"https://www.ideals.illinois.edu/oai-pmh"},"display":{"title":"Coordination and Catalysis of the Lambda Integrase Site -Specific Recombination Reaction","abstract":"In the course of my doctoral work, I have developed quantitative assays to measure the maximal cleavage and ligation activity of Integrase. From this work, we concluded that para-Nitrophenol tyrosine analogs are optimal for quantitative in vitro measurement of Int ligation. Int could not utilize tyrosine analogs para-Cresol and dimethyl- p-phenylenediamine as ligation substrates under my reaction conditions. However, they may be useful to identify and characterize Int or other tyrosine recombinase proteins with enhanced ligation activities.","abstract_html":"In the course of my doctoral work, I have developed quantitative assays to measure the maximal cleavage and ligation activity of Integrase. From this work, we concluded that para-Nitrophenol tyrosine analogs are optimal for quantitative in vitro measurement of Int ligation. Int could not utilize tyrosine analogs para-Cresol and dimethyl- p-phenylenediamine as ligation substrates under my reaction conditions. 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