Literature DB >> 2943282

Type 1, 2A, and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers.

D Danieli Betto, E Zerbato, R Betto.   

Abstract

Mammalian skeletal muscles are mixture of three type of fibers: type 1, type 2A, and type 2B fibers. Immunological studies and proteolytic analysis of myosin heavy chains from the three type of fibers have demonstrated the presence of distinct myosin isoforms. By using typed single muscle fibers and improving an electrophoretic method we are able to resolve three distinct polypeptides which are demonstrate to correspond to type 1, 2A and 2B myosin heavy chain isoforms by using specific monoclonal antibodies. The analysis of single muscle fibers shows that different myosin heavy chain isoforms are frequently coexpressed in the same muscle fiber.

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Year:  1986        PMID: 2943282     DOI: 10.1016/s0006-291x(86)80592-7

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  53 in total

1.  Myosin heavy-chain composition in striated muscle after tenotomy.

Authors:  A Jakubiec-Puka; C Catani; U Carraro
Journal:  Biochem J       Date:  1992-02-15       Impact factor: 3.857

2.  Force-velocity relations and myosin heavy chain isoform compositions of skinned fibres from rat skeletal muscle.

Authors:  R Bottinelli; S Schiaffino; C Reggiani
Journal:  J Physiol       Date:  1991-06       Impact factor: 5.182

3.  Enhanced athletic performance on multisite AAV-IGF1 gene transfer coincides with massive modification of the muscle proteome.

Authors:  Antero Macedo; Manuela Moriggi; Michele Vasso; Sara De Palma; Mauro Sturnega; Giorgio Friso; Cecilia Gelfi; Mauro Giacca; Serena Zacchigna
Journal:  Hum Gene Ther       Date:  2012-01-26       Impact factor: 5.695

4.  Myosin heavy chain composition of single fibres from normal human muscle.

Authors:  D Biral; R Betto; D Danieli-Betto; G Salviati
Journal:  Biochem J       Date:  1988-02-15       Impact factor: 3.857

5.  ATP utilization for calcium uptake and force production in different types of human skeletal muscle fibres.

Authors:  P Szentesi; R Zaremba; W van Mechelen; G J Stienen
Journal:  J Physiol       Date:  2001-03-01       Impact factor: 5.182

6.  Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibres.

Authors:  R Bottinelli; R Betto; S Schiaffino; C Reggiani
Journal:  J Physiol       Date:  1994-07-15       Impact factor: 5.182

7.  Myosin, parvalbumin and myofibril expression in barbel (Barbus barbus L.) lateral white muscle during development.

Authors:  B Focant; F Huriaux; P Vandewalle; M Castelli; G Goessens
Journal:  Fish Physiol Biochem       Date:  1992-08       Impact factor: 2.794

8.  Exercise training induces transitions of myosin isoform subunits within histochemically typed human muscle fibres.

Authors:  H Baumann; M Jäggi; F Soland; H Howald; M C Schaub
Journal:  Pflugers Arch       Date:  1987-08       Impact factor: 3.657

9.  Maximum shortening velocity and coexistence of myosin heavy chain isoforms in single skinned fast fibres of rat skeletal muscle.

Authors:  R Bottinelli; R Betto; S Schiaffino; C Reggiani
Journal:  J Muscle Res Cell Motil       Date:  1994-08       Impact factor: 2.698

10.  Changes in fibre-type composition and myosin heavy-chain IId isoform in rat soleus muscle during recovery period after hindlimb suspension.

Authors:  Y Oishi; H Yamamoto; E Miyamoto
Journal:  Eur J Appl Physiol Occup Physiol       Date:  1994
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