Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis Metadata

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Title

  • Main Title Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis

Creator

  • Author: Stawska, Agnieszka A.
    Creator Type: Personal

Contributor

  • Chair: O'Donovan, Gerard A.
    Contributor Type: Personal
    Contributor Info: Major Professor
  • Committee Member: Benjamin, Robert C.
    Contributor Type: Personal
  • Committee Member: Zimmerman, Earl G.
    Contributor Type: Personal

Publisher

  • Name: University of North Texas
    Place of Publication: Denton, Texas

Date

  • Creation: 2001-08
  • Digitized: 2007-07-09

Language

  • English

Description

  • Content Description: The enzyme, aspartate transcarbamoylase (ATCase) from Moraxella (Branhamella) catarrhalis, has been purified. The holoenzyme has a molecular mass of approximately 510kDa, harbors predominantly positive charges and is hydrophobic in nature. The holoenzyme possesses two subunits, a smaller one of 40 kDa and a larger one of 45 kDa. A third polypeptide has been found to contribute to the overall enzymatic activity, having an approximate mass of 55 kDa. The ATCase purification included the generation of cell-free extract, streptomycin sulfate cut, 60 °C heat step, ammonium sulfate cut, dialysis and ion, gel-filtration and hydrophobic interaction chromatography. The enzyme's performance throughout purification steps was analyzed on activity and SDS-PAGE gradient gels. Its enzymatic, specific activities, yield and fold purification, were also determined.

Subject

  • Library of Congress Subject Headings: Pyrimidine nucleotides -- Metabolism.
  • Library of Congress Subject Headings: Moraxella.
  • Keyword: Aspartate transcarbamoylase
  • Keyword: Enzyme purification
  • Library of Congress Subject Headings: Moraxella (Branhamella) catarrhalis

Collection

  • Name: UNT Theses and Dissertations
    Code: UNTETD

Institution

  • Name: UNT Libraries
    Code: UNT

Rights

  • Rights Access: public
  • Rights License: copyright
  • Rights Holder: Stawska, Agnieszka A.
  • Rights Statement: Copyright is held by the author, unless otherwise noted. All rights reserved.

Resource Type

  • Thesis or Dissertation

Format

  • Text

Identifier

  • OCLC: 51243955
  • Archival Resource Key: ark:/67531/metadc2864

Degree

  • Degree Name: Master of Science
  • Degree Level: Master's
  • Degree Discipline: Molecular Biology
  • Academic Department: Department of Biological Sciences
  • Degree Grantor: University of North Texas

Note

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