Literature DB >> 4550711

The myosin filament. IV. Observation of the internal structural arrangement.

F A Pepe, B Drucker.   

Abstract

The subunit organization of the myosin filament of chicken striated muscle has been observed directly in cross-sections in electron microscopy. The organization consists of three centrally located and nine peripherally located subunits in a close-packed arrangement. This arrangement is that predicted by a previously derived model for the detailed molecular organization of the myosin filament (Pepe, 1966 a, 1967 a, 1971). Each subunit measures approximately 30 A in diameter and the center-to-center distance is approximately 37 A. If these measurements are considered to be on the high side, then they indicate that each subunit represents one myosin molecule. However, it is not possible to determine unequivocally whether one or two myosin molecules per subunit are present on the basis of this work.

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Year:  1972        PMID: 4550711      PMCID: PMC2108639          DOI: 10.1083/jcb.52.2.255

Source DB:  PubMed          Journal:  J Cell Biol        ISSN: 0021-9525            Impact factor:   10.539


  13 in total

1.  Conformation of individual macromolecular particles from myosin solution.

Authors:  R V RICE
Journal:  Biochim Biophys Acta       Date:  1961-09-30

2.  The myosin filament. I. Structural organization from antibody staining observed in electron microscopy.

Authors:  F A Pepe
Journal:  J Mol Biol       Date:  1967-07-28       Impact factor: 5.469

3.  Substructure of the myosin molecule. I. Subfragments of myosin by enzymic degradation.

Authors:  S Lowey; H S Slayter; A G Weeds; H Baker
Journal:  J Mol Biol       Date:  1969-05-28       Impact factor: 5.469

4.  The myosin filament. II. Interaction between myosin and actin filaments observed using antibody staining in fluorescent and electron microscopy.

Authors:  F A Pepe
Journal:  J Mol Biol       Date:  1967-07-28       Impact factor: 5.469

5.  Ultrastructure of insect flight muscle. I. Screw sense and structural grouping in the rigor cross-bridge lattice.

Authors:  M K Reedy
Journal:  J Mol Biol       Date:  1968-01-28       Impact factor: 5.469

6.  A reevaluation of the Markham rotation technique using model systems.

Authors:  M H Friedman
Journal:  J Ultrastruct Res       Date:  1970-08

7.  The low-angle x-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor.

Authors:  H E Huxley; W Brown
Journal:  J Mol Biol       Date:  1967-12-14       Impact factor: 5.469

8.  [Perplexities and confirmations concerning the problem of the structure of muscular myosin filaments].

Authors:  B Baccetti
Journal:  Boll Soc Ital Biol Sper       Date:  1966-09-30

9.  The mass of myosin per cross-bridge in insect fibrillar flight muscle.

Authors:  R A Chaplain; R T Tregear
Journal:  J Mol Biol       Date:  1966-11-14       Impact factor: 5.469

10.  An electron microscope study of canine cardiac myosin and some of its aggregates.

Authors:  J A Carney; A L Brown
Journal:  J Cell Biol       Date:  1966-02       Impact factor: 10.539

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  3 in total

1.  The myosin filament XIV backbone structure.

Authors:  F T Ashton; J Weisel; F A Pepe
Journal:  Biophys J       Date:  1992-06       Impact factor: 4.033

2.  Three-dimensional structure of frozen-hydrated paracrystals of myosin rod.

Authors:  R Ward; J M Murray
Journal:  J Muscle Res Cell Motil       Date:  1990-10       Impact factor: 2.698

3.  Paracrystals of myosin rod.

Authors:  R Ward; P M Bennett
Journal:  J Muscle Res Cell Motil       Date:  1989-02       Impact factor: 2.698

  3 in total

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