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

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...

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Detalles Bibliográficos
Autores principales: Stromer, Marvin H., Hartshorne, D. J., Mueller, Helmut, Rice, Robert V.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1969
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2107591/
https://www.ncbi.nlm.nih.gov/pubmed/5782443
Descripción
Sumario: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 α-actinin or a combination of α-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.