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  • 1
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 50 (1993), S. 863-874 
    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 method was developed to measure the adhesion between fibers and fast curing elastomer, in droplet form, using the microbond pull-out method. Samples were fabricated by arranging the fibers as a grid on which elastomer droplets were formed for testing. A droplet sliding test method was developed to investigate the nature of the sites of the droplets on the fiber after displacement of the droplets. Fibers of polyester, aramid, and HMW-polyethylene were tested with resins of polyurethane and natural rubber latex. The fibers had been surface-treated by corona, gamma radiation, or methanol extraction. The shape of the droplets was determined by microscopic measurement. The shear strength of the fiber/matrix bond was tested using a microvise grip in a tensile strength tester. © 1993 John Wiley & Sons, Inc.
    Additional Material: 16 Ill.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 53 (1993), S. 206-212 
    ISSN: 0730-2312
    Keywords: NADPH-cytochrome P-450 oxidoreductase ; rat epidermis ; reconstitution with P-450 1A1 ; immunohisto-chemistry ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: NADPH-cytochrome P-450 oxidoreductase (P-450 red) transfers reducing equivalents from NADPH to cytochrome P-450 (P-450) in the monooxygenase system. Detergent solubilized proteins from the membrane fraction of neonatal rat epidermis were purified by 2′,5′-ADP-agarose affinity column chromatography. The purified protein showed an apparent homogeneity on sodium dodecylsulfate-polyacrylamide gel electrophoresis and molecular weight was estimated to be 78 kDa. NADPH-cytochrome c reductase activity increased by 95-fold in the purified enzyme. Epidermal P-450 red in vitro reconstituted benzo(a)pyrene hydroxylase activity in a dose dependent manner with P-450 purified from either rat liver or epidermis. Western blot analysis demonstrated that epidermal P-450 red immunologically cross reacts to liver P-450 red. Immunohistochemical staining showed that the enzyme was predominantly localized in the epidermis. The intensity of immunohistochemical staining of rat skin sections and tissue distribution did not change in the skin treated with β-naphtoflavone, which results in a substantial increase in P-450 1A1 activity. Quantitative assessment of P-450 red in treated and untreated epidermis also showed no change. These findings indicate that constitutive P-450 red, fully capable of supporting P-450, exists in rat epidermis, and can function in metabolism of endogenous and exogenous compounds.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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