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  • Articles: DFG German National Licenses  (13)
  • 1980-1984  (6)
  • 1970-1974  (7)
  • 11
    Electronic Resource
    Electronic Resource
    Influence of the xyloadenosine analogue of 2′,5′-oligoriboadenylate on poly(A)-specific, 2′,5′-oligoriboadenylate degrading 2′,3′-exoribonuclease and further enzymes involved in poly(A)(+)mRNA metabolism (1984)
    Springer
    Molecular biology reports 10 (1984), S. 83-89 
    Details
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract The homogeneous poly(A)-specific 2′,3′-exoribonuclease from calf thymus gland, which cleaves both 3′,5′-and 2′,5′-linked oligoriboadenylates, does not degrade (xyloA2'p)2 xyloA, the xylofuranosyladenosine analogue of the 2-5A core. This oligonucleotide, which is supposed to enter intact cells rapidly, was found to possess an increased stability and an enhanced antiherpesvirus activity compared to the natural (A2'p)2A (Eppstein, D. A., Barnett, J. W., Marsh, Y. V., Gosselin, G. and Imbach, J.-L. (1983) Nature 302, 723–724). The poly(A) anabolic enzyme, poly(A) polymerase (Mn2+-dependent), from the same source, which is initiated by (A3'p)2A and its higher oligomers, does not accept 2–5A core and its xyloadenosine analogue as primer. Both oligonucleotides exert no influence on endoribonuclease IV and on the integrity of the poly(A)-ribonucleoprotein complex.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00776979
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    Paper (German National Licenses)
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  • 12
    Electronic Resource
    Electronic Resource
    Interaction of polyribosomal components and polyribonucleotides with microtubule proteins (1982)
    Springer
    Molecular biology reports 8 (1982), S. 233-237 
    Details
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To demonstrate the affinity of RNA-containing polyribosomal components (isolated from L5178y cells) to microtubules, microtubule protein was attached to an insoluble matrix. In contrast to ribosomes, poly(A) (+) mRNA and poly(A)-RNP were found to bind to the matrix. Using synthetic polyribonucleotides, no significant differences in the binding properties of single- and double stranded polymers of different base composition to microtubule protein were observed. However, binding is dependent on the size of the polymer; a minimal chain length of 12 nucleotide units is required.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00776585
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    Paper (German National Licenses)
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  • 13
    Electronic Resource
    Electronic Resource
    Fibronectin is apparently not involved in species-specific reaggregation of cells from the marine sponge geodia cydonium (1982)
    New York, N.Y. : Wiley-Blackwell
    Journal of Cellular Biochemistry 19 (1982), S. 395-404 
    Details
    ISSN: 0730-2312
    Keywords: fibronectin ; sponges ; Geodia cydonium ; aggregation ; cell recognition ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Experiments were carried out to test the hypothesis that fibronectin is involved in reaggregation of dissociated sponge cells. Cells from the siliceous sponge Geodia cydonium were extracted with urea to solubilize fibronectin from cells of higher multicellular organisms. The crude extract was further fractionated by DNA, heparin, and collagen affinity chromatography; they were termed Geodia fibronectinlike fractions. The fibronectinlike fractions contained a series of proteins with molecular weights different from that of the genuine fibronectin. The Geodia fibronectinlike fractions did not react with antiserum, produced against human fibronectin, under formation of a precipitin line. Using this antiserum the sponge cells could not be specifically labeled with FITC-anti-IgG antiserum. Radioimmunoprecipitation experiments revealed that the Geodia fractions contain - if at all - 0.1% fibronectin or fibronectinlike protein at the most. In the crucial experiments it was shown that the Geodia fibronectinlike fractions, human fibronectin, and antifibronectin antiserum exerted no influence on adhesion of Geodia cells either in the absence or in the presence of the soluble aggregation factor. Based on these findings, we conclude that fibronectin is apparently not present on Geodia cells and does not play a role in aggregation of this biological system.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jcb.240190408
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    Paper (German National Licenses)
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