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The Journal of Cell Biology, Vol 40, 167-178, Copyright © 1969 by Rockefeller University Press

ARTICLE

THE EFFECT OF VARIOUS PROTEIN FRACTIONS ON Z- AND M-LINE RECONSTITUTION

Marvin H. Stromer 1, D. J. Hartshorne 1, Helmut Mueller 1, and Robert V. Rice 1

1 From the Mellon Institute of Carnegie-Mellon University, Pittsburgh, Pennsylvania 15213.

Dr. Stromer's present address is the Department of Animal Science, Iowa State University, Ames, Iowa 50010

Extraction of thin, glycerinated bundles of rabbit psoas muscle with a low ionic strength solvent results in removal first of M lines and then of Z lines. When these extracted myofibrillar bundles are allowed to interact, at adjusted ionic conditions, with the dilute myofibrillar extract or with the fractions obtained at 40% ammonium sulfate saturation from either the myofibrillar extract or from the Bailey extract of natural actomyosin, reconstitution of Z lines occurs. The ammonium sulfate fraction from the Bailey extract of natural actomyosin restores the tetragonal lattice structure of the Z line. Other structural features such as I-band tufts or cross-bridges, M lines and H-zone binding also occur with some of the proteins used for recombination. Although it has not yet been possible to identify exactly the protein(s) constituting the Z line, it appears unlikely that tropomyosin or troponin alone is the major protein of the Z line. A more likely candidate is alpha-actinin or a combination of alpha-actinin with another protein(s). In addition, this study demonstrates that basic morphological differences exist between cross-sections through the Z-line lattice and cross-sections through tropomyosin crystals.

Submitted on June 6, 1968
Revised on August 6, 1968


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