Abstract
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.