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  • 1
    ISSN: 1432-2048
    Keywords: Chloroplast (electron transport) ; Heat stress ; Membrane organisation ; Pisum (electron transport and heat stress)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Exposure of isolated chloroplasts of pea (Pisum sativum L.) to temperatures above 35° C leads to a stimulation of photosystem-I-mediated electron transport from dichlorophenolindophenol to methyl viologen. The threshold temperature for this stimulation coincides closely with that for heat-induced inhibition of photosystem-II activity in such chloroplasts. This coincidence is explained in terms of a rearrangement of the thylakoid membrane resulting in the exposure of a new set of donor sites for dichlorophenolindophenol within the cytochrome f/b 6 complex of the electron-transport chain linking the two photosystems.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of bioenergetics and biomembranes 17 (1985), S. 217-223 
    ISSN: 1573-6881
    Keywords: Ca2+-ATPase ; sarcoplasmic reticulum ; calcium transport ; fatty acids ; membrane organization
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of palmitic and oleic acids on Ca2+-ATPase activity in coupled preparations of sarcoplasmic reticulum isolated from rabbit hind leg muscle have been compared with their effects on vesicles uncoupled with Ca2+ ionophore, A23187. Palmitate at 2 µM · mg protein−1 has no significant effect on enzyme activity and does not uncouple catalytic activity from calcium accumulation within the vesicles. Oleic acid at 1 µM · mg protein−1 uncouples the vesicles, whereas 2 µM · mg protein−1 completely inhibits Ca2+-ATPase activity. Fluorescence anisotropy of diphenylhexatriene is not significantly altered by palmitate, but a large transient increase in motion of the probe is observed with addition of oleic acid. The effects of oleic acid on enzyme activity are not mediated via an effect on the bulk properties of the hydrophobic domain of the membrane lipids.
    Type of Medium: Electronic Resource
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