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  • 1980-1984  (3)
  • 1
    Electronic Resource
    Electronic Resource
    Myosin light chains of avian and mammalian slow muscles: peptide mapping of 2S light chains (1984)
    Springer
    Journal of muscle research and cell motility 5 (1984), S. 411-421 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The 2S light chains of mammalian and avian slow muscle myosin, indistinguishable by two-dimensional gel electrophoresis, have been examined by peptide mapping. The fragments obtained withS. aureus V8 protease were analysed either by gel electrophoresis or by reverse-phase high performance liquid chromatography. The peptide maps of avian 2S light chains contain fragments distinct from those of mammalian 2S light chains. Chicken and turkey LC2S appear to be more similar to each other than those from mammalian species (rat and rabbit). These results are in agreement with the relative phylogenetic distances among the four species studied here. The 2S light chain of slow muscle represent further examples of polypeptides which comigrate in two-dimensional gel electrophoresis in spite of their different peptide maps.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00818259
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Myosin light chains of avian and mammalian slow muscles: evidence of intraspecific polymorphism (1981)
    Springer
    Journal of muscle research and cell motility 2 (1981), S. 335-342 
    Details
    ISSN: 1573-2657
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary The myosin light chains of slow muscles from different species have been examined with two-dimensional gel electrophoresis. While the myosin light chain 2S of mammalian soleus muscles (rabbit, rat and guinea-pig) could not be distinguished from that of avian anterior latissimus dorsi (chicken and turkey), the 1S light chain complement of myosins shows inter- and intraspecific differences. The 1S light chain varies between birds and mammals. The 1'S light chain is absent in avian slow myosins and has an electrophoretic mobility peculiar to each mammalian species. Furthermore the relative amount of 1'S and 1S light chains varies in different muscles of the same mammalian species and among species.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00713271
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    Paper (German National Licenses)
    Fulltext
  • 3
    Electronic Resource
    Electronic Resource
    Light and heavy chains of myosin from atrial and ventricular myocardium of turkey and rat (1983)
    Springer
    Basic research in cardiology 78 (1983), S. 671-678 
    Details
    ISSN: 1435-1803
    Keywords: rat ; turkey ; myosin polymorphism ; atrial myosin ; ventricular myosin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary Subunit composition of myosins from atrial and ventricular cardiac muscle of turkey and rat was examined by two-dimensional polyacrylamide electrophoresis of light chains and by peptide mapping of electrophoretically purified heavy chains. In regard to light subunits in two-dimensional electrophoresis, the corresponding light chains from atrial and ventricular myocardium comigrate in the turkey. By contrast the atrial light chains LC1 and LC2 are easily distinguishable from the corresponding subunits of the ventricles in the rat. The peptide patterns of myosin heavy chains from atrial and ventricular cells were different both in turkey and rat, indicating differences in their primary structures. Therefore atrial and ventricular myosins differ in heavy chains composition in all the avian and mammalian species so far studied, suggesting that this heterogeneity represents a general feature related to the different physiological properties of atrial and ventricular cardiac cells.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01907214
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    Paper (German National Licenses)
    Fulltext
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