Structures with the characteristics of molecular myosin were identified by electron microscopy in tissue sections of vertebrate smooth muscle. No thick filaments of myosin were found regardless of preparative procedures, which included fixation at rest and in contraction, glycerine extraction, and storage at low pH prior to fixation. Absence of thick myosin filaments and presence of what appear to be myosin molecules is in accord with conclusions based on X-ray diffraction (3, 12) and birefringence data (4) from living smooth muscles at rest and in contraction. Explanations are provided for appearances thought by others (6, 20, 21) to represent thick myosin filaments. Our present observations are in accord with the model for smooth muscle contraction which we have previously proposed (1).
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1 January 1970
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January 01 1970
LOCUS AND STATE OF AGGREGATION OF MYOSIN IN TISSUE SECTIONS OF VERTEBRATE SMOOTH MUSCLE
Bernard J. Panner,
Bernard J. Panner
From the Departments of Pathology and Physiology, University of Rochester, School of Medicine and Dentistry, Rochester, New York 14620
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Carl R. Honig
Carl R. Honig
From the Departments of Pathology and Physiology, University of Rochester, School of Medicine and Dentistry, Rochester, New York 14620
Search for other works by this author on:
Bernard J. Panner
From the Departments of Pathology and Physiology, University of Rochester, School of Medicine and Dentistry, Rochester, New York 14620
Carl R. Honig
From the Departments of Pathology and Physiology, University of Rochester, School of Medicine and Dentistry, Rochester, New York 14620
Received:
May 19 1969
Revision Received:
August 19 1969
Online ISSN: 1540-8140
Print ISSN: 0021-9525
Copyright © 1970 by The Rockefeller University Press.
1970
J Cell Biol (1970) 44 (1): 52–61.
Article history
Received:
May 19 1969
Revision Received:
August 19 1969
Citation
Bernard J. Panner, Carl R. Honig; LOCUS AND STATE OF AGGREGATION OF MYOSIN IN TISSUE SECTIONS OF VERTEBRATE SMOOTH MUSCLE . J Cell Biol 1 January 1970; 44 (1): 52–61. doi: https://doi.org/10.1083/jcb.44.1.52
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