Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis

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.

Grantor dc:publisher

University of North Texas

Year dc:date

2001

Author dc:creator

• Stawska, Agnieszka A.

Contributors dc:contributor

• O'Donovan, Gerard A.
• Benjamin, Robert C.
• Zimmerman, Earl G.

• Pyrimidine nucleotides -- Metabolism.
• Moraxella.
• Moraxella catarrhalis
• Aspartate transcarbamoylase
• Subunits
• Holoenzyme
• Enzyme purification

Statement dc:rights

• Public
• Copyright
• Stawska, Agnieszka A.
• Copyright is held by the author, unless otherwise noted. All rights reserved.

Language dc:language

English

Identifier

oclc: 51243955
https://digital.library.unt.edu/ark:/67531/metadc2864/
ark: ark:/67531/metadc2864

OAI identifier oai:identifier

info:ark/67531/metadc2864