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  • 1
    Electronic Resource
    Electronic Resource
    Human cardiac and skeletal muscle spectrins: Differential expression and localization (1992)
    New York, NY : Wiley-Blackwell
    Cell Motility and the Cytoskeleton 21 (1992), S. 293-304 
    Details
    ISSN: 0886-1544
    Keywords: erythroid spectrin ; non-erythroid spectrin ; Z-line ; membrane ; neuromuscular junction ; developmental changes ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Medicine
    Notes: We describe multiple human cardiac and skeletal muscle spectrin isoforms. Cardiac muscle expresses five erythroid α,β spectrin-reactive isoforms with estimated MR's of 280, 274, 270, 255, and 246 kD, respectively At least one nonerythroid α-spectrin of MR 284 kD is expressed in heart. While skeletal muscle shares the 280, 270, and 246 kD erythroid spectrins, it expresses an immunologically distinct 284 kD nonerythroid α-spectrin isoform. The 255 kD erythroid β-spectrin isoform is specific for cardiac tissue. By immunocytochemistry, both erythroid β- and nonerythroid α-spectrins are localized to costameres, the plasma membrane, and the neuromuscular junctional region.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/cm.970210405
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  • 2
    Electronic Resource
    Electronic Resource
    Interaction of myosin and paramyosin (1975)
    New York, N.Y. : Wiley-Blackwell
    Journal of Supramolecular Structure 3 (1975), S. 354-360 
    Details
    ISSN: 0091-7419
    Keywords: Life Sciences ; Molecular Cell Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: The interaction of myosin and paramyosin was investigated by enzymological and ultrastructural techniques. The actin-activated Mg+2 ATPase of rabbit skeletal muscle myosin can be inhibited by clam adductor paramyosin. Both proteins must be rapidly coprecipitated to form filaments for this inhibition. Slowly formed cofilaments are fully activatable by F-actin. In both cases, the cofilaments possess unique structural characteristics when compared to homofilaments.The mode of inhibition appears to be competitive when different concentrations of paramyosin and F-actin are compared. The apparent affinity of the myosin heads for actin is reduced by the presence of paramyosin within rapidly reconstituted thick filaments. These results suggest that paramyosin may serve as part of a relaxing mechanism within invertebrate muscles. It is unlikely that paramyosin plays a role in the initiation and maintenance of catch within specialized molluscan muscles.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jss.400030407
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    Paper (German National Licenses)
    Fulltext
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