The molecular basis for the mechanism of contraction in striated muscle, with primary emphasis on the interaction between the thick and thin filaments and the role of the thin (actin) filaments, is the theme presented. Recent information relating to actin-myosin interaction points up the fact that definitive statements cannot be made regarding the molecular interaction(s) that lead to contraction. Nevertheless, the properties of actin indicate that (a) actin in the monomeric state has properties differing markedly from actin in the polymer (filament) state; (b) these property differences may be significant in the contractile process, for they include changes in the reactivity of the bound nucleotide and actin-myosin complex formation; (c) the bound nucleotide seems to be required in the contraction process. For these, and other, reasons discussed, the tentative hypothesis is advanced that the contraction reaction involves local changes in the actin filament providing local monomer or monomer-like actin units in the reaction with myosin.
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1 July 1967
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July 01 1967
Reactivities of Actin as a Contractile Protein
Teru Hayashi
Teru Hayashi
From the Department of Biological Sciences, Columbia University, New York, and the Marine Biological Laboratory, Woods Hole, Massachusetts.
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Teru Hayashi
From the Department of Biological Sciences, Columbia University, New York, and the Marine Biological Laboratory, Woods Hole, Massachusetts.
Dr. Hayashi's present address is the Biology Department, Illinois Institute of Technology, Chicago
Online ISSN: 1540-7748
Print ISSN: 0022-1295
Copyright © 1967 by The Rockefeller University Press
1967
J Gen Physiol (1967) 50 (6): 119–133.
Citation
Teru Hayashi; Reactivities of Actin as a Contractile Protein . J Gen Physiol 1 July 1967; 50 (6): 119–133. doi: https://doi.org/10.1085/jgp.50.6.119
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