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  • 1
    Electronic Resource
    Electronic Resource
    Mutations in a hydrophilic part of the core gene of hepatitis C virus in patients with hepatocellular carcinoma in China (1997)
    Springer
    Journal of gastroenterology 32 (1997), S. 47-55 
    Details
    ISSN: 1435-5922
    Keywords: HCV ; missense mutation ; hepatocellular carcinoma ; CTL ; China
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We investigated the association between hepatocellular carcinoma (HCC) and the genomic characteristics of the hepatitis C virus (HCV) isolated from residents of the inshore region of the Yangtze River, an area that has one of the highest incidence of HCC in China. We determined the genomic heterogeneity of HCV, and the sequence divergence of the HCV core gene in individuals with chronic hepatitis and HCC. HCV genotype II was predominant among these isolates, which were homologous to other Chinese and Japanese HCV isolates. The rate of nucleotide substitutions in the core gene was significantly greater for isolates from HCC patients than for those from individuals with chronic hepatitis. The nucleotide substitutions were unevenly scattered along the core gene; a cluster of missense mutations was apparent in the region encoding the second hydrophilic domain of the core protein. The rate of occurrence of missense mutations per nucleotide substitution was significantly greater in this clustering variable region (CVR) of the core gene than in the remaining core gene sequence. These observations suggest that mutations in the CVR may be involved in the pathogenesis of chronic HCV infection during hepatocellular carcinogenesis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01213296
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    Paper (German National Licenses)
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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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