THE ULTRASTRUCTURE OF STRIATED MUSCLE AT VARIOUS SARCOMERE LENGTHS | Zendy

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THE ULTRASTRUCTURE OF STRIATED MUSCLE AT VARIOUS SARCOMERE LENGTHS

Author(s) -

David Spiro

Publication year - 1956

Publication title -

the journal of cell biology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.414

H-Index - 380

eISSN - 1540-8140

pISSN - 0021-9525

DOI - 10.1083/jcb.2.4.157

Subject(s) - sarcomere , actin , biology , ultrastructure , myofilament , myosin , biophysics , myofibril , anatomy , muscle contraction , myocyte , microbiology and biotechnology , biochemistry

1. Rest and equilibrium length muscle sarcomeres are composed of thin filaments (actin) which traverse the sarcomeres from the Z membranes up to the H band; at this level the filaments are considerably thicker and less numerous. 2. Shortening of muscle is associated with a transformation of thin into thick filaments in the A band. 3. These observations are discussed in terms of interaction of actin and myosin to form a supercoiled structure as the basis of contraction.

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