Coordination and Catalysis of the Lambda Integrase Site -Specific Recombination Reaction
Kazmierczak, Robert Andrew
This item is only available for download by members of the University of Illinois community. Students, faculty, and staff at the U of I may log in with your NetID and password to view the item. If you are trying to access an Illinois-restricted dissertation or thesis, you can request a copy through your library's Inter-Library Loan office or purchase a copy directly from ProQuest.
Permalink
https://hdl.handle.net/2142/86671
Description
Title
Coordination and Catalysis of the Lambda Integrase Site -Specific Recombination Reaction
Author(s)
Kazmierczak, Robert Andrew
Issue Date
2004
Doctoral Committee Chair(s)
Gardner, Jeffrey F.
Department of Study
Microbiology
Discipline
Microbiology
Degree Granting Institution
University of Illinois at Urbana-Champaign
Degree Name
Ph.D.
Degree Level
Dissertation
Keyword(s)
Biology, Molecular
Language
eng
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.
Use this login method if you
don't
have an
@illinois.edu
email address.
(Oops, I do have one)
IDEALS migrated to a new platform on June 23, 2022. If you created
your account prior to this date, you will have to reset your password
using the forgot-password link below.