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  • 1980-1984  (2)
  • 1975-1979  (2)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 39 (1983), S. 58-59 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Laser diffraction intensity decrease in active muscles precedes tension development at sarcomere lenghts below 2.76 μm, but not at greater lenghts. This suggests that the time lag is caused by random sarcomere shortenings inside each myofibril.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Cellular and molecular life sciences 31 (1975), S. 241-243 
    ISSN: 1420-9071
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Zusammenfassung Fucose-reiches Glykoprotein wurde aus Eierstockpseudomucin isoliert. Mit Hilfe spezifischer Anti-Glykoprotein-Seren wurde die Antigenizität der Pseudomucine mit Immunoelektrophorese und die Ouchterlony Methode untersucht.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Histochemistry and cell biology 76 (1982), S. 107-112 
    ISSN: 1432-119X
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Glycoproteins were isolated from human gastric mucosa, and their reactivities with concanavalin A, periodate oxidation and subsequent reduction, are described. Gastric glycoproteins corresponding to the paradoxical concanavalin A staining-class II and III mucins were proved biochemically. The analytical results suggest that N-acetylglucosamine residues in the glycoproteins mediate the interaction with concanavalin A.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 3 (1975), S. 333-337 
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Myosin catalyzed exchange between 32Pi and ATP in reaction medium during its enzymatic hydrolysis of ATP only by a very small amount. Addition of actin increased to a great extent the rate of incorporation of 32Pi in the presence of Mg. Glycerinated smooth muscle fibers also exhibited the ability to exchange 32Pi and ATP upon the application of external force (repeated stretching and releasing). A schematic mechanism of the action of actin and external force on acceleration of 32Pi incorporation is proposed and the importance of the M*-ADP complex for force generation is suggested.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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