Browsing by Author "den Camp, Huub J. M. O."

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    The Level of Enzymes Involved In the Allantoin Metabolism of Bacillus Fastidiosus Grown under Different Conditions
    (Springer Link, 1995) Muruke, Masoud S. H.; den Camp, Huub J. M. O.; Semesi, Amelia K.; van der Drift, Chris
    Bacillus fastidiosus was cultivated in batch and continuous culture on various carbon and nitrogen sources. The enzymes involved in allantoin degradation (allantoinase, urease, carboligase) of B. fastidiosus were hardly affected by either carbon or nitrogen source. In contrast, the enzymes involved in glycerol utilization (glycerol kinase, glycerol 3-phosphate dehydrogenase) were induced during growth on glycerol, but were not affected by the amount of allantoin present.
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    Novel Nitrogen Sources for Growth of Bacillus Fastidiosus and their Effect on the Activity of NADP-Dependent Glutamate Dehydrogenase
    (1993) Muruke, Masoud S. H.; den Camp, Huub J. M. O.; van der Drift, Chris
    Although Bacillus fastidiosus assimilates ammonium formed internally during growth on urate, allantoin or allantoate via NADP-dependent glutamate dehydrogenase (NADP-GDH), growth on exogenous ammonium as nitrogen source has not been observed. Growth on ammonium, urea and ureidoglycolate, intermediates of the urate degradative pathway, was found to occur if the mineral growth medium containing glycerol as a carbon source was supplemented with both allantoin (0.5 mM) and brain heart infusion (BHI, 0.1%, w/v) or yeast extract. Neither allantoin nor BHI supported growth alone or in combination unless ammonium was present. NADP-GDH activity appeared to be regulated only by the extracellular concentration of allantoin or allantoate. Enzyme activity was not influenced by other nitrogen sources or the intracellular ammonium concentration.
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    Rapid Purification of Uricase from Bacillus Fastidiosus
    (1996) Muruke, Masoud S. H.; den Camp, Huub J. M. O.; van der Drift, Chris
    A simple, rapid procedure was developed for the purification of uricase from Bacillus fastidiosus. The enzyme was purified to homogeneity in a two-step procedure with the aid of fast-flow column chromatography. In this way high yields (37 %) of pure uricase with a specific activity of 78.3 U/mg were obtained in a short time.