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  • Purification  (2)
  • Cerebrovascular reactivity  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Effects of peritumoural oedema on cerebral blood flow and cerebrovascular reactivity in patients with alert consciousness (1999)
    Springer
    European journal of nuclear medicine 26 (1999), S. 1493-1496 
    Details
    ISSN: 1619-7089
    Keywords: Key words: Cerebral blood flow ; Cerebrovascular reactivity ; Cerebral oedema ; Brain tumour ; Acetazolamide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract. The effects of peritumoural oedema on cerebral blood flow (CBF) and cerebrovascular reactivity (CVR) were studied in 18 patients with alert consciousness. Hemispheric mean CBF was measured by performing first-pass radionuclide angiography using technetium-99m hexamethylpropylene amine oxime. CVR was measured as the percentage change from the baseline mean CBF value after acetazolamide administration. Patients were classified into three groups according to the severity of peritumoural oedema. The mean CBF of both hemispheres in each group was not significantly different from that of age-matched controls. CVR was preserved in patients with mild peritumoural oedema (n=6), but was significantly (P〈0.01) reduced in patients with moderate (n=7) and severe peritumoural oedema (n=5). No significant correlation was found between the degree of midline shift and the mean CVR of both hemispheres (P=0.09). Surgical removal of the tumour significantly (P〈0.05) improved the impaired CVR, although the mean CBF did not change. Administration of glucocorticoid improved the impaired CVR, without a change in the mean CBF, in a patient with a metastatic brain tumour. We conclude that CVR is impaired by the development of peritumoural oedema prior to changes in mean CBF.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002590050485
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  • 2
    Electronic Resource
    Electronic Resource
    Purification and properties of mangano-superoxide dismutase from a strain of alkaliphilic Bacillus (1997)
    Springer
    Extremophiles 1 (1997), S. 74-78 
    Details
    ISSN: 1433-4909
    Keywords: Key words Superoxide dismutase ; Purification ; Alkaliphile ; Bacillus
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A mangano-superoxide dismutase (EC 1.15.1.1) was purified to homogeneity from a strain of alkaliphilic Bacillus for the first time. The purified protein, with an isoelectric point of pH 4.5, had a molecular mass of approximately 50 kDa and consisted of two identical subunits (25 kDa). The N-terminal amino acid sequence was Ala-Tyr-Lys-Leu-Pro-Glu-Leu-Pro-Tyr-Ala-Ala-Asn-Ala-Leu-Glu-Pro-His-Ile-Asp-Glu-Ala. The optimum pH and temperature for the reaction were 7.5 and 35°C, respectively. The properties of the superoxide dismutase were compared with those of the enzyme from thermophilic Bacillus stearothermophilus.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050017
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Thermostable alkaline cellulase from an alkaliphilic isolate, Bacillus sp. KSM-S237 (1997)
    Springer
    Extremophiles 1 (1997), S. 151-156 
    Details
    ISSN: 1433-4909
    Keywords: Key wordsBacillus ; Alkaliphilic ; Alkaline ; Thermo-stable ; Cellulase ; Purification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Thermostable alkaline cellulase (endo-1,4-β-glucanase, EC 3.2.1.4) activity was detected in the culture medium of a strictly alkaliphilic strain of Bacillus, designated KSM-S237. This novel enzyme was purified to homogeneity by a two-step column-chromatographic procedure with high yield. The N-terminal amino acid sequence of the purified enzyme was Glu-Gly-Asn-Thr-Arg-Glu-Asp-Asn-Phe-Lys-His-Leu-Leu-Gly-Asn-Asp-Asn-Val-Lys-Arg. The enzyme had a molecular mass of approximately 86 kDa and an isoelectric point of pH 3.8. The enzyme had a pH optimum of 8.6–9.0 and displayed maximum activity at 45°C. The alkaline enzyme was stable up to 50°C and more than 30% of the original activity was detectable after heating at 100°C and at pH 9.0 for 10 min. The enzyme hydrolyzed carboxymethylcellulose, lichenan (β-1,3;1,4-linkage), and p-nitrophenyl derivatives of cellotriose and cellotetraose. Crystalline forms of cellulose (Avicel and filter paper), H3PO4-swollen cellulose, NaOH-swollen cellulose, curdlan (β-1,3-linkage), laminarin (β-1,3;1,6-linkage), and xylan were barely hydrolyzed at all.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s007920050028
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    Paper (German National Licenses)
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