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Title:Coordination and Catalysis of the Lambda Integrase Site -Specific Recombination Reaction
Author(s):Kazmierczak, Robert Andrew
Doctoral Committee Chair(s):Gardner, Jeffrey F.
Department / Program:Microbiology
Discipline:Microbiology
Degree Granting Institution:University of Illinois at Urbana-Champaign
Degree:Ph.D.
Genre:Dissertation
Subject(s):Biology, Molecular
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.
Issue Date:2004
Type:Text
Language:English
Description:97 p.
Thesis (Ph.D.)--University of Illinois at Urbana-Champaign, 2004.
URI:http://hdl.handle.net/2142/86671
Other Identifier(s):(MiAaPQ)AAI3153348
Date Available in IDEALS:2015-09-28
Date Deposited:2004


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