Dissertation (Ph.D.)--University of Toledo, 2009. / ["In partial fulfillment of the requirements for the degree of Doctor of Philosophy in Biomedical Sciences."] Title from title page of PDF document. Bibliography: p. 80-112.

Thesis (Ph. D.) -- University of Texas Southwestern Medical Center at Dallas, 2004. / Vita. Bibliography: 214-244.

Diss. (sammanfattning) Umeå : Univ., 2003. / Härtill 4 uppsatser.

Thesis (M.S.)--University of Toledo, 2008. / "In partial fulfillment of the requirements for the degree of Master of Science in Biomedical Sciences." Title from title page of PDF document. Non-Latin script record Bibliography: pages 74-92.

Moraxella (Branhamella) catarrhalis, although commonly isolated from sputum in patients with pneumonia, rarely causes bacteremia. Sodium polyanethol sulfonate is commonly added to routine blood culture media to increase the yield of Gram-negative bacilli. This anticoagulant also inhibits the growth of Neisseria meningitidis. We added strains f Moraxella (Branhamella) catarrhalis to routine blood culture media supplemented with 0.03% SPS. No inhibitory effect could be demonstrated. The rare occurrence of bacteremic Moraxella (Branhamella) catarrhalis pneumonia is not due to an inhibitory effect of routine blood culture media.

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.

Thesis (Ph. D.) -- University of Texas Southwestern Medical Center at Dallas, 2006. / Embargoed. Vita. Bibliography: 194-220.