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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Biotechnology and Bioengineering 24 (1982), S. 971-975 
    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
    Library Location Call Number Volume/Issue/Year Availability
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  • 2
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Archives of Insect Biochemistry and Physiology 1 (1983), S. 1-15 
    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
    Library Location Call Number Volume/Issue/Year Availability
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