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  • 1
    Electronic Resource
    Electronic Resource
    Once-daily pantoprazole 40 mg and esomeprazole 40 mg have equivalent overall efficacy in relieving GERD-related symptoms (2003)
    Oxford, UK : Blackwell Science Ltd
    Alimentary pharmacology & therapeutics 18 (2003), S. 0 
    Details
    ISSN: 1365-2036
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Aim : To compare the efficacy of pantoprazole and esomeprazole for the treatment of gastro-oesophageal reflux disease- (GERD-) related symptoms.Methods : In this multicentre, randomized, double-blind study 217 patients [intention-to-treat (ITT) population] diagnosed with endoscopically proven GERD grade B/C received pantoprazole (40 mg once daily (o.d.), n = 112] or esomeprazole (40 mg o.d/, n = 105) for 4 weeks. Patients recorded GERD-related symptoms (daytime and night-time) using diaries (daily), and/or by telephone interviews (every third day) and completed the Gastrointestinal Symptom Rating Scale (GSRS) questionnaire. The area under the time curve (AUC) for the sum score of GERD-related symptoms (symptom load of each patient during the treatment) and the time to reach adequate relief from GERD-related symptoms were calculated.Results : Patients reported first adequate relief from daytime GERD-related symptoms after a mean of 3.7 (pantoprazole) and 5.9 days (esomeprazole) (P = 0.034); the values for the night-time were 1.7 and 3.5 days, respectively (P = 0.012, ITT). The AUCs for the single symptoms and the sum scores were comparable.Conclusions : Treatment with pantoprazole resulted in significantly faster first-time relief from daytime and night-time GERD-related symptoms than esomeprazole. Pantoprazole and esomeprazole were similar with respect to reduction of load of GERD-related symptoms.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1365-2036.2003.01745.x
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  • 2
    Electronic Resource
    Electronic Resource
    Ammonia-Forming Cytochrome c Nitrite Reductase from Sulfurospirillum deleyianum Is a Tetraheme Protein: New Aspects of the Molecular Composition and Spectroscopic Properties
    Amsterdam : Elsevier
    Biochemical and Biophysical Research Communications 205 (1994), S. 911-916 
    Details
    ISSN: 0006-291X
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1006/bbrc.1994.2751
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  • 3
    Electronic Resource
    Electronic Resource
    Characterization of the membranous denitrification enzymes nitrite reductase (cytochrome cd1) and copper-containing nitrous oxide reductase from Thiobacillus denitrificans (1996)
    Springer
    Archives of microbiology 165 (1996), S. 55-61 
    Details
    ISSN: 1432-072X
    Keywords: Key words Cytochrome cd1 ; Nitrite reductase ; Nitrous ; oxide reductase ; Denitrification ; Thiobacillus ; denitrificans ; Pseudomonas stutzeri ; DNA hybridization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Cytochrome cd 1-nitrite reductase and nitrous oxide reductase of Thiobacillus denitrificans were purified and characterized by biochemical and immunochemical methods. In contrast to the generally soluble nature of the denitrification enzymes, these two enzymes were isolated from the membrane fraction of T. denitrificans and remained active after solubilization with Triton X-100. The properties of the membrane-derived enzymes were similar to those of their soluble counterparts from the same organism. Nitrous oxide reductase activity was inhibited by acetylene. Nitrite reductase and nitrous oxide reductase cross-reacted with antisera raised against the soluble enzymes from Pseudomonas stutzeri. The nirS, norBC, and nosZ genes encoding the cytochrome cd 1-nitrite reductase, nitric oxide reductase, and nitrous oxide reductase, respectively, from P. stutzeri hybridized with genomic DNA from T. denitrificans. Cross-reactivity and similar N-terminal amino acid and gene sequences suggest that the primary structures of the Thiobacillus enzymes are homologous to the soluble proteins from P. stutzeri.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s002030050296
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    Paper (German National Licenses)
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