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  • Biochemistry and Biotechnology  (3)
  • Stomoxys calcitrans  (2)
  • Aspirin central action  (1)
  • 1
    Electronic Resource
    Electronic Resource
    Effects of diflubenzuron and tunicamycin on N-acetylglucosaminyl transferases in prepupae of the stable fly (Stomoxys calcitrans) (1985)
    Springer
    Cellular and molecular life sciences 41 (1985), S. 623-625 
    Details
    ISSN: 1420-9071
    Keywords: Stable fly ; Stomoxys calcitrans ; diflubenzuron ; tunicamycin ; N-acetylglucosaminyl transferase ; prepupae
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Tunicamycin, an antibiotic, and diflubenzuron, an insect growth regulator, were tested to determine their effects on N-acetylglucosaminyl transferase fromS. calcitrans prepupae. Diflubenzuron had no effect, but tunicamycin inhibited the transfer of GlcNAc-1-P from UDP-GlcNAc to dolicholmonophosphate with an I50 of 1.5–4 ng/ml.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02007689
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Aspirin analgesia evaluated by event-related potentials in man: Possible central action in brain (1980)
    Springer
    Experimental brain research 39 (1980), S. 359-364 
    Details
    ISSN: 1432-1106
    Keywords: Pain ; Brain-evoked potentials ; Aspirin central action
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The mechanism of aspirin analgesia is still unclear, but it is generally assumed that aspirin exerts its analgesic effect mainly on peripheral nociceptors. In this study, we demonstrate possible brain effects of 975 mg aspirin in man. When brain electrical potentials evoked by painful electrical tooth shocks were examined, aspirin was observed to significantly reduce the amplitude of the late waveform components, but it did not affect the earlier components. Since our earlier findings suggest that early waveform components reflect the energy transmission and the late components manifest the brain activities in an individual's perception of painful information, we postulate that aspirin may act centrally in pain processing.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00239300
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Potentiometric method for subatrate analysis using immobilized NAD+-dependent oxidoreductase enzymes (1979)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 21 (1979), S. 1905-1915 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Two coenzyme-dependent oxidoreductases, glucose dehydrogenase and alcohol dehydrogenase, were immobilized in polyacrylamide gel over a platinum grid matrix and used as enzyme electrodes to measure their substrate concentrations in buffered aqueous solutions. The immobilized enzymes were used to oxidize their substrates in the presence of NAD+. Ferricyanide was used as the redox mediator and electroactive specific. The determinations of glucose and ethenol were utilized to demonstrate and evaluate the performance of the system. The described methodology should be readily applicable to the analysis of numerous other substrates of coenzyme-dependent oxidoreductases.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260211103
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Potentiometric quantitation of glycerol using immobilized glycerol dehydrogenase (1982)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 971-975 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Glycerol dehydrogenase was immobilized in polyacrylamide gel layered over a small platinum screen and used to catalyze the oxidation of glycerol. In the presence of NAD+ and potassium ferricyanide, the coupling reaction generated a measurable electrical potential which was found to be Nernstian with respect to the glycerol concentration range of 10-4M to 10-1M. The reproducibility of the measurement and the optimal conditions for glycerol determination were described.
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260240416
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Electrochemical evaluation of lactate dehydrogenase immobilized in polyacrylamide gels (1977)
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 19 (1977), S. 1785-1792 
    Details
    ISSN: 0006-3592
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Lactate dehydrogenase (EC 1.1.1.27) has been immobilized in polyacrylamide gels over a platinum grid matrix. The immobilized enzyme is used to oxidize L-lactate in the presence of nicotinamide adenine dinucleotide (NAD+) and femcyanide. The NADH produced is then chemically oxidized back to NAD+by ferricyanide. The coupled reduction of ferricyanide ions to ferrocyanide ions results in a measurable electrochemical potential. This measurable zero-current potential is found to be Nernstian in nature and directly proportional to the logarithm values of L-Iactate concentration over the range of 2 × 10-5to 5 × 10-2M. The results indicate that immobilized lactate dehydrogenase can be incorporated into a system to detect L-Lactate acid in aqueous solutions.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/bit.260191205
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Characterization of mannosyl transferases during the pupal instar of Stomoxys calcitrans (L) (1983)
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 1 (1983), S. 1-15 
    Details
    ISSN: 0739-4462
    Keywords: Stomoxys calcitrans ; mannosyl transferase ; stable fly ; glycosyl transferase ; dolicholphosphate ; Chemistry ; Food Science, Agricultural, Medicinal and Pharmaceutical Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: Particulate fractions (10,000g) from pupae of Stomoxys calcitrans transfer [14C]-mannose from GDP-[14C]-mannose to dolichol monophosphate and proteins. Production of the mannosyl lipid was inhibited by Mn2+, UDP, GMP, GDP, and EDTA. The insect growth regulator diflubenzuron had no effect on mannosyl transferase activity. Dolichol monophosphate and Mg2+ stimulated mannosyl transferase activity. The mannosyl lipid product was identified as mannosyl-phosphoryl-dolichol (Man-P-Dol). The apparent Km and Vmax values for the formation of Man-P-Dol using GDP-[14C]-Man while holding dolichol phosphate constant were 2.4 ± 0.9 μM and 9.4 ± 2.3 pmol Man-P-Dol·min-1·mg-1 protein, respectively. The apparent Km and Vmax values using dólichol phosphate while holding GDP-Man constant were 2.2 ± 1.2 μM and 18.5 ± 1.7 pmol Man-P-Dol·min-1·mg-1 protein.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/arch.940010102
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    Paper (German National Licenses)
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