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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 55 (1995), S. 1317-1327 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: A calorimetric study for estimating crosslinking densities of polydimethylsiloxane (PDMS) networks is presented. It involves the experimental determination of the heat capacities of the polymer with (Cip) and without (C0p) crosslinking. The theoretical basis of the method is described as well as the procedure used for the determination of the Cps. The crosslinking densities of PDMS networks, determined by absorbency (swelling) measurments, using the Flory-Rehner equation, and by the method described here, are compared. The PDMS, obtained by the anionic synthesis of octamethylcyclotetrasiloxane, was analyzed by gel permeation chromatography and infrared spectroscopy. Separate samples of the polymer were further crosslinked at different network densities. The Cps and the thermal stabilities were determined by DSC and TGA, respectively. The results indicate that the crosslinking density ratios of the polymer networks calculated by the relation ΔCip/C0p are in reasonable agreement with those obtained from absorbency measurements. The crosslinking density can also be obtained from heat capacity measurments if the density of the network is known at the temperature that ΔCp is obtained. © 1995 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 10 (1995), S. 285-289 
    ISSN: 0884-3996
    Keywords: Cholinesterase ; luminol ; pro-enhancer ; chemiluminescence ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: 2-Naphthyl acetate acts as a pro-enhancer of the luminol-H2O2-horseradish peroxidase reaction. Cholinesterase hydrolyses the bound acetyl group and produces 2-naphthol, and this compound is an enhancer of the chemiluminescent reaction. We studied the kinetics of chemiluminescent emission and the influence of 2-naphthyl acetate and cholinesterase enzyme concentration. The cholinesterase concentration versus chemiluminescence intensity maximum was linear for cholinesterase between 0 and 181 μU/mL, with a detection limit of 8 μU/mL and a relative standard deviation of 9.5% (n = 3), for a sample containing 90.67 μU/mL of cholinesterase.
    Additional Material: 5 Ill.
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  • 3
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 10 (1995), S. 175-184 
    ISSN: 0884-3996
    Keywords: Luminol ; enhanced chemiluminescence ; phenolic acid ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: We explored the behaviour of a series of phenolic acids used as enhancers or inhibitors of luminol chemiluminescence by three different methods to determine if behaviour was associated with phenolic acid structure and redox character. All the phenolic acids inhibited chemiluminescence when hexacyanoferrate(III) was reacted with the phenolic acids before adding luminol. The redox character of these compounds was clearly related to structure. When hexacyanoferrate(III)-luminol-O2 chemiluminescence was initiated by phenolic acid-luminol mixtures some phenolic acids behaved as enhancers of chemiluminescence, and others as inhibitors. We propose a mechanism to explain these findings. We found direct relationships between the redox character of the phenolic acids and the enhancement or inhibition of the chemiluminescence of the luminol-H2O2-peroxidase system and we propose mechanism to explain these phenomena.
    Additional Material: 7 Ill.
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Journal of Bioluminescence and Chemiluminescence 13 (1998), S. 75-84 
    ISSN: 0884-3996
    Keywords: luminol ; enhanced chemiluminescence ; phenol ; Chemistry ; Biochemistry and Biotechnology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Systematic studies on phenol derivatives facilitates an explanation of the enhancement or inhibition of the luminol-H2O2-horseradish peroxidase system chemiluminescence. Factors that govern the enhancement are the one-electron reduction potentials of the phenoxy radicals (PhO•/PhOH) vs. luminol radicals (L•/LH-) and the reaction rates of the phenol derivatives with the compounds of horseradish peroxidase (HRP-I and HRP-II). Only compounds with radicals with a similar or greater reduction potential than luminol at pH 8.5 (0.8 V) can act as enhancers. Radicals with reduction potentials lower than luminol behave in a different way, because they destroy luminol radicals and inhibit chemiluminescence. The relations between the reduction potential, reaction rates and the Hammett constant of the substituent in a phenol suggest that 4-substituted phenols with Hammett constants (σ) for their substituents similar or greater than 0.20 are enhancers of the luminol-H2O2-horseradish peroxidase chemiluminescence. In contrast, those phenols substituted in position 4 for substituents with Hammett constants (σ) lower than 0.20 are inhibitors of chemiluminescence. On the basis of these studies, the structure of possible new enhancers was predicted. © 1998 John Wiley & Sons, Ltd.
    Additional Material: 3 Ill.
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