Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis

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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 ... continued below

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Stawska, Agnieszka A. August 2001.

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  • Stawska, Agnieszka A.

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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.

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  • August 2001

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  • Sept. 25, 2007, 10:38 p.m.

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  • Oct. 9, 2008, 11:59 a.m.

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Stawska, Agnieszka A. Purification of Aspartate Transcarbamoylase from Moraxella (Branhamella) catarrhalis, thesis, August 2001; Denton, Texas. (digital.library.unt.edu/ark:/67531/metadc2864/: accessed October 18, 2017), University of North Texas Libraries, Digital Library, digital.library.unt.edu; .