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University of Illinois at Urbana-Champaign

Coordination and Catalysis of the Lambda Integrase Site -Specific Recombination Reaction

Abstract

dc:description

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.

Degree

thesis:*
Name thesis:degree_name
Ph.D.
Level thesis:degree_level
Dissertation
Discipline thesis:degree_discipline
Microbiology
Grantor
University of Illinois at Urbana-Champaign
Year dc:date
2015

Author and committee

dc:creator, dc:contributor.*
Author dc:creator
  • Kazmierczak, Robert Andrew
Contributors dc:contributor
  • Gardner, Jeffrey F.

Subjects

dc:subject × 1

Rights

Language dc:language
eng

Identifiers

dc:identifier.*
Identifier
(MiAaPQ)AAI3153348
OAI identifier oai:identifier
oai:www.ideals.illinois.edu:2142/86671

Chain of custody

source
Harvested from
University of Illinois - Urbana-Champaign
Base URL
www.ideals.illinois.edu/oai-pmh
Last updated
2026-07-22
Source record
OAI-PMH GetRecord
citation

Kazmierczak, Robert Andrew. Coordination and Catalysis of the Lambda Integrase Site -Specific Recombination Reaction. Dissertation thesis, University of Illinois at Urbana-Champaign, 2015. http://hdl.handle.net/2142/86671