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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Russian chemical bulletin 45 (1996), S. 18-25 
    ISSN: 1573-9171
    Keywords: horseradish peroxidase ; reaction mechanisms ; substrate-substrate activation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The structure and functions of peroxidases are characterized. Attention is focused on the mechanisms of action of horseradish peroxidase in reactions with different substrates and on correlations between structure and functions of various heme-containing proteins. The phenomenon of substrate-substrate activation typical of peroxidase-catalyzed reactions is discussed.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 8 (1988), S. 461-464 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Tween 80 and proteose peptone effect on cellulase production with Trichoderma spec. was studied. Sugar cane pith was used in the medium as carbon source. Tween 80 increases cellulase production while proteose peptone has influence on enzyme adsorption. There is a combined effect on cellulase production between them.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 6 (1991), S. 139-145 
    ISSN: 0884-3996
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 6 (1991), S. 137-138 
    ISSN: 0884-3996
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 4 (1989), S. 406-418 
    ISSN: 0884-3996
    Keywords: Firefly luciferase ; luminescence ; enzyme kinetics ; bioluminescence spectra ; allosteric activators ; firefly mRNA translation ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Biochemical properties, spectral parameters of bioluminescence and reaction kinetics for Luciola mingrelica firefly luciferase are described and analysed. The kinetic scheme of the enzymatic process is proposed and discussed. Allosteric regulation of luciferase activity by ATP and its analogues is considered and binding Mg2+ to luciferase shown to increase its activity. Regulation mechanism of luciferase activity by phospholipids is analysed and choline-containing phospholipids shown to be specific luciferase activators. Some properties of firefly luciferae and the luciferase synthesized during firefly mRNA translation in frog oocytes are compared.
    Additional Material: 12 Ill.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 4 (1989), S. 419-422 
    ISSN: 0884-3996
    Keywords: Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Allowing for the lipid nature of firefly luciferase we have developed a new method for obtaining high-activity and high-stability enzyme preparations for bioluminescent microassay. The method includes the step of differential centrifugation in presence of stabilizing additives which entails a partial purification of the enzyme and its essential stabilization likely due to the fact that luciferase retains its lipid environment which plays an important role in catalysis. The resultant luciferase preparation is stable in solution at 4 °C for 2-3 months and allows the detection of down to 10-11M ATP.A new method has been offered for luciferase immobilization on film carriers precoated with a phospholipid layer. By sorption of the enzyme on such carriers, the samples of immobilized luciferase have been obtained suitable for constructing chemiluminescent biosensors, in the form of luciferase-containing films. There are many-fold applications for detection of ATP micro-quantities.
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
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