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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Molecular genetics and genomics 217 (1989), S. 53-59 
    ISSN: 1617-4623
    Keywords: Transposable elements ; Transgenic tobacco ; Maize ; Transformation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A two component maize transposon system comprising a stable but trans-active Ac element and a cis responsive Ds element has been established in transgenic tobacco. The development of this system is desirable for the realization of a gene tagging strategy employing these elements in heterologous plant species. Transgenic tobacco with a single transposed Ac element (Ac-18) which has sustained a 4 bp terminal deletion has been identified. Transposase activity of the stable Ac-18 was demonstrated in a tissue culture assay as well as in transgenic plants. When plants containing Ac-18 were crossed with transgenic plants carrying a Ds element, 25%–50% of the F1 progeny showed trans-activation of Ds transposition. Analysis of DNA of several F1 plants showed that each plant displayed a unique pattern of Ds transposition to new chromosomal sites.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 7 (1977), S. 419-434 
    ISSN: 0091-7419
    Keywords: peroxisome ; microbody ; nucleoid core ; urate oxidase ; starvation effects ; rat liver enzymes ; catalase ; cell organelle ; Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The appearance of the characteristic crystalloid core of rat liver peroxisomes is emulated by the electron microscopic (EM) appearance of highly purified urate oxidase prepared from the same tissue. The purity of the enzyme preparation was established by gel electrophoresis under various conditions and the specific enzyme activity was at least as high as any previously reported. The amino acid composition of urate oxidase was determined. As additional evidence for close association of the peroxisomal core with urate oxidase, it was demonstrated that the biphasic changes in rat liver urate oxidase activity in response to prolonged starvation were paralleled by changes in the EM appearance of peroxisomes. Under comparable conditions catalase, another peroxisomal enzyme, did not show the same changes in activity as did urate oxidase. Evidence for the possible identity of urate oxidase with the peroxisomal crystalloid of rat liver has been presented, all materials having been obtained from, and experiments performed with, the rat.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
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