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  • Springer  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Characterization and fibre type distribution of a new myofibrillar protein of molecular weight 32 kDa (1986)
    Springer
    Journal of muscle research and cell motility 7 (1986), S. 517-526 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A new basic protein of molecular weight 32 kDa has been isolated and purified to homogeneity from skeletal muscles rich in type I fibres. By the use of a specific monoclonal antibody, the protein has been shown to be present in all type I fibres and some type II fibres, the number of which varies with the muscle and the region of the muscle sectioned. A protein of similar properties could not be isolated from rabbit muscles consisting predominantly of type II fibres. By fluorescence microscopy, the protein has been shown to be located in the Z-disc from which the presence of divalent cations, probably calcium, facilitates its extraction at low ionic strength. The protein is unusual in that its distribution does not correlate completely with the known muscle fibre types and in that as yet there is no evidence for the presence of an isoform in those cells that do not stain with the specific antibody for the 32 kDa protein isolated from slow muscles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01753568
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  • 2
    Electronic Resource
    Electronic Resource
    The effect of denervation on the distribution of the polymorphic forms of troponin components in fast and slow muscles of the adult rat (1982)
    Springer
    Cell & tissue research 225 (1982), S. 201-215 
    Details
    ISSN: 1432-0878
    Keywords: Troponin I, T and C ; Denervation ; Skeletal muscle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary In the soleus muscle of the normal rat the number of cells containing fast troponin I decreased and those containing slow troponin I increased after birth until less than 10% stained for the fast form in the adult muscle. On denervation of soleus muscle this pattern of change was reversed with the result that the majority of cells stained for fast troponin I. The change was more rapid when denervation was carried out at 12 weeks rather than at 52 weeks of age. Denervation of extensor digitorum longus and tibialis anterior muscles produced little change in the distribution of fast and slow troponin I over a period of 12 weeks. After long periods (〉24 weeks) of denervation of these fast muscles, fast troponin I was observed in cells in which originally only slow troponin I could be detected. Similar results to those obtained with troponin I in both fast and slow muscles were obtained using antibodies to the fast and slow forms of troponin C and troponin T.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00216229
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    Paper (German National Licenses)
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