1,720,983 research outputs found
Myosin light and heavy chains in rat gastrocnemius and diaphragm muscles after chronic denervation or reinnervation
No full textMyosin light and heavy chains in rat gastrocnemius and diaphragm muscles after chronic denervation or reinnervation.
Carraro U, Catani C, Dalla Libera L.
Exp Neurol. 1981 May;72(2):401-12. No abstract available.
PMID:
7238699
[PubMed - indexed for MEDLINE
Myosin light chains of avian and mammalian slow muscles: evidence of intraspecific polymorphism
No full textThe 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. © 1981 Chapman and Hall Ltd
Myosin light chains of avian and mammalian slow muscles: peptide mapping of 2S light chains.
No full textJ Muscle Res Cell Motil. 1984 Aug;5(4):411-21.
Myosin light chains of avian and mammalian slow muscles: peptide mapping of 2S light chains.
Dalla Libera L, Betto R, Lodolo R, Carraro U.
Abstract
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 with S. 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.
PMID:
6384262
[PubMed - indexed for MEDLINE
Chronic denervation of rat diaphragm: Selective maintenance of adult fast myosin heavy chains
No full textAfter long‐term denervation in mixed rat muscles there is a selective loss of slow myosin. The bidimensional electrophoretic pattern of light chains and the results of preliminary studies on heavy chains have left open the question of whether the nature of the residual fast‐like myosin is of the immature or adult type. We have further investigated chronically denervated myosin by (1) electrophoresis in nondissociating conditions; (2) acidic electrophoresis of the heavy chains; and (3) proteolytic mapping of the heavy chains. These techniques clearly distinguish adult myosins from those present in immature muscles. Using these criteria, myosin from the chronically denervated diaphragm is of an adult type, even though the presence of trace amounts of embryonic myosin cannot be excluded. The contractile properties also indicate that chronically denervated hemidiaphragm is more similar to an adult fast muscle than to an immature muscle. The selective maintenance after long‐term denervation..
Stress response as a tool to monitor and to counteract progression of muscular atrophy. Validation of Oxyblot techniques using microbiopsies.
No full textImmunological and biochemical differences between atrial and ventricular myosins in vertebrates.
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