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  • Blackwell Publishing Ltd  (3)
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  • 1
    Digitale Medien
    Digitale Medien
    Effects of Carbon Source, Gibberellins and Ethylene on Wall-Bound Invertase Activity in Callus of Convolvulus arvensis (1974)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 30 (1974), S. 0 
    Details
    ISSN: 1399-3054
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: The growth rate of Convolvulus callus on a sucrose-containing medium appeared to be largely independent of the activity of cell wall invertase. The increase of this enzyme activity which occurs upon subculturing was unaffected within the first 24 h by the presence of the substrate sucrose. Neither substitution by glucose or fructose, nor complete deletion of the carbon source had any effect.Gibberellins apparently were not involved in the initiation and/or control of the increase of wall-bound invertase activity occurring upon subculturing. Exogenous ethylene was unable to mimick this effect of subculturing but when applied immediately after subculturing it had a synergistic effect on the increase of invertase. Inhibition occurred, however, when exposure to ethylene was delayed until after 24 h of incubation. These findings suggest a role of ethylene in the control of wall-bound invertase activity.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1399-3054.1974.tb03667.x
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    α-Glucosidase Activity Located at the Cell Surface in Callus of Convolvulus arvensis (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 25 (1971), S. 0 
    Details
    ISSN: 1399-3054
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: Cell wall preparations of Convolvulus callus were found to contain α-glucosidase activity, the bulk of which could be solubilized by solutions of high ionic strength. Callus tissue incubated in 0.5 M KC1 released α-glucosidase activity into the washing medium as distinct from tissue incubated in 1.0 M sorbitol. The wall-bound activity of KCl-treated tissue was found to be less than that of sorbitol-treated tissue, while the difference between both activities proved to be equal to the enzyme activity found in the washing medium of KCl-treated tissue. Since no trace of cell leakage was observed, it is concluded that α-glucosidase activity is located at the cell surface. The level of this surface-located enzyme was not affected by the presence of maltose in the nutrient medium.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1399-3054.1971.tb01438.x
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Wall-bound Invertase Activity in Convolvulus Callus: Increase after Subculturing, and Paradoxical Effects of Actinomycin D, Cycloheximide, and Thienylalanine (1972)
    Oxford, UK : Blackwell Publishing Ltd
    Physiologia plantarum 26 (1972), S. 0 
    Details
    ISSN: 1399-3054
    Quelle: Blackwell Publishing Journal Backfiles 1879-2005
    Thema: Biologie
    Notizen: The wall-bound invertase activity increased 3.3-fold upon transfer of fragments of Convolvulus callus to fresh solid nutrient medium and 7.7-fold upon transfer to liquid nutrient medium. Addition of actinomycin D, cycloheximide or the amino acid analogue thienylalanine brought about a further stimulation of the invertase content of the cell walls. The rise of wall-bound invertase activity was not due to redistribution of invertase activity between cytoplasm and cell walls, and appeared to be dependent on metabolic energy.An equation is presented to calculate the half-life of enzymes from their time-course. Applied on the time-courses of wall-bound invertase activity, a half-life of about 12 h was obtained in callus transferred to fresh solid medium and of about 5.4 h in tissue transferred to liquid medium. It is argued that the increase of invertase content of the cell walls is due to an enhanced rate of invertase synthesis.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1111/j.1399-3054.1972.tb01123.x
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