Isolation and Characterization of the Operon Containing Aspartate Transcarbamoylase and Dihydroorotase from Pseudomonas aeruginosa

PDF Version Also Available for Download.

Description

The Pseudomonas aeruginosa ATCase was cloned and sequenced to determine the correct size, subunit composition and architecture of this pivotal enzyme in pyrimidine biosynthesis. During the course of this work, it was determined that the ATCase of Pseudomonas was not 360,000 Da but rather present in a complex of 484,000 Da consisting of two different polypeptides (36,000 Da and 44,000 Da) with an architecture similar to that of E. coli ATCase, 2(C3):3(r2). However, there was no regulatory polypeptide found in the Pseudomonas ATCase.

Physical Description

vii, 206 leaves: ill.

Creation Information

Vickrey, John F. (John Fredrick), 1959- May 1993.

Context

This dissertation is part of the collection entitled: UNT Theses and Dissertations and was provided by UNT Libraries to Digital Library, a digital repository hosted by the UNT Libraries. It has been viewed 49 times . More information about this dissertation can be viewed below.

Who

People and organizations associated with either the creation of this dissertation or its content.

Publisher

Rights Holder

For guidance see Citations, Rights, Re-Use.

  • Vickrey, John F. (John Fredrick), 1959-

Provided By

UNT Libraries

With locations on the Denton campus of the University of North Texas and one in Dallas, UNT Libraries serves the school and the community by providing access to physical and online collections; The Portal to Texas History and UNT Digital Libraries; academic research, and much, much more.

Contact Us

What

Descriptive information to help identify this dissertation. Follow the links below to find similar items on the Digital Library.

Degree Information

Description

The Pseudomonas aeruginosa ATCase was cloned and sequenced to determine the correct size, subunit composition and architecture of this pivotal enzyme in pyrimidine biosynthesis. During the course of this work, it was determined that the ATCase of Pseudomonas was not 360,000 Da but rather present in a complex of 484,000 Da consisting of two different polypeptides (36,000 Da and 44,000 Da) with an architecture similar to that of E. coli ATCase, 2(C3):3(r2). However, there was no regulatory polypeptide found in the Pseudomonas ATCase.

Physical Description

vii, 206 leaves: ill.

Language

Identifier

Unique identifying numbers for this dissertation in the Digital Library or other systems.

Collections

This dissertation is part of the following collection of related materials.

UNT Theses and Dissertations

Theses and dissertations represent a wealth of scholarly and artistic content created by masters and doctoral students in the degree-seeking process. Some ETDs in this collection are restricted to use by the UNT community.

What responsibilities do I have when using this dissertation?

When

Dates and time periods associated with this dissertation.

Creation Date

  • May 1993

Added to The UNT Digital Library

  • March 26, 2014, 9:30 a.m.

Description Last Updated

  • Jan. 30, 2015, 1:41 p.m.

Usage Statistics

When was this dissertation last used?

Yesterday: 0
Past 30 days: 3
Total Uses: 49

Interact With This Dissertation

Here are some suggestions for what to do next.

Start Reading

PDF Version Also Available for Download.

International Image Interoperability Framework

IIF Logo

We support the IIIF Presentation API

Vickrey, John F. (John Fredrick), 1959-. Isolation and Characterization of the Operon Containing Aspartate Transcarbamoylase and Dihydroorotase from Pseudomonas aeruginosa, dissertation, May 1993; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc278859/: accessed July 22, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .