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  • 1985-1989  (3)
  • 1985  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Oxford [u.a.] : International Union of Crystallography (IUCr)
    Acta crystallographica 41 (1985), S. 415-417 
    ISSN: 1600-5759
    Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001
    Topics: Chemistry and Pharmacology , Geosciences , Physics
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1420-9071
    Keywords: Rat liver ; cytochrome oxidase ; mitochondria ; BW755C ; 3, amino-1-[m-(trifluoromethyl)phenyl]-2-pyrazoline ; lipoxygenase inhibitor ; cyclo-oxygenase inhibitor
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The interaction between BW755C (3-amino-1-[m-(trifluoromethyl)phenyl]-2-pyrazoline), a potent inhibitor of both lipoxygenase and cyclo-oxygenase, and respiratory chain in mitochondria and electron transport particles (ETP) from rat livers was examined. BW755C accelerated the oxygen uptake by mitochondria without the addition of substrate for the respiratory chain. Spectrophotometric study revealed that BW755C was quickly oxidized by cytochrome oxidase in mitochondria to a compound possessing an absorption maximum at 524 nm. p-Phenylenediamine (p-diaminobenzene, PPDA), which, like BW755C, serves as an electron donor to cytoschrome oxidase, was shown to inhibit the generation of active oxygen in macrophages; the inhibition was stronger than that of BW755C. These results strongly suggest that the oxidative conversion of BW755C by mitochondrial cytochrome oxidase is associated with its potentially inhibitory action on the active oxygen-generating system in phagocytes.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 82 (1985), S. 345-350 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The localization and distribution of peroxidase (PPO) activity were studied ultracytochemically in thrombocytes from lampreys, carps, frogs, snakes, tortoises, rabbits, sheep, dogs, and monkeys. PPO activity was not deteetable in the thrombocytes of lampreys, carps, frogs, and snakes. However, this enzyme activity was demonstrated in the nuclear envelope and endoplasmic reticulum of tortoise thrombocytes. Dog and monkey thrombocytes (blood platelets) exhibited PPO activity in the dense tubular system, but this enzyme activity was not detectable in rabbit and sheep thrombocytes. Our observations are interpreted to suggest that thrombocytes from animals lower than amphibia are peroxidase negative. Furthermore, it can be said that thrombocytes from animals higher than reptiles are generally positive, although there are exceptions. PPO activity was localized in the endoplasmic-reticulum system, but not in the cytoplasmic granules of thrombocytes common to submammals and mammals. In this study, we also compared the distribution of peroxidase activity in thrombocytes, neutrophils, and eosinophils and conclude that these are significant differences in the distribution of PPO and myeloperoxidase.
    Type of Medium: Electronic Resource
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