Takahashi K, Hattori A
Department of Animal Science, Faculty of Agriculture, Hokkaido University, Sapporo, Hokkaido.
J Biochem. 1989 Apr;105(4):529-36. doi: 10.1093/oxfordjournals.jbchem.a122701.
The relationship between the ultrastructure and protein components of Z-disks was studied using psoas muscles of rabbit and breast muscles of chicken. Glycerinated fiber bundles of these muscles were treated with a solution containing 0.1 mM Ca2+ to induce a structural weakening of Z-disks non-enzymatically. During the treatment, clear geometrical configurations of Z-filaments could be observed along with removal of amorphous matrix under an electron microscope. Even after a prolonged treatment for 14 d in which all Z-disks were entirely weakened, entangled Z-filaments were left in the original region of the disks. Immunoelectron microscopic observations showed that antibodies against alpha-actinin bound to the entangled Z-filaments, forming dense lines at the position of the original Z-disks. On SDS-PAGE of Z-disk substances, alpha-actinin remained unchanged and Mr 75,000 and 55,000 proteins were removed during the Ca2+-treatment. We therefore conclude that alpha-actinin is a component of Z-filaments, and that the amorphous matrix is composed at least of these Mr 75,000 and 55,000 proteins.
利用兔的腰大肌和鸡的胸肌研究了Z盘的超微结构与蛋白质成分之间的关系。将这些肌肉的甘油化纤维束用含0.1 mM Ca2+的溶液处理,以非酶方式诱导Z盘的结构弱化。在处理过程中,在电子显微镜下可以观察到Z细丝的清晰几何构型以及无定形基质的去除。即使在长达14天的所有Z盘完全弱化的长时间处理后,缠结的Z细丝仍留在盘的原始区域。免疫电子显微镜观察表明,抗α-辅肌动蛋白抗体与缠结的Z细丝结合,在原始Z盘的位置形成致密线。在Z盘物质的SDS-PAGE上,α-辅肌动蛋白保持不变,而Mr 75,000和55,000的蛋白质在Ca2+处理过程中被去除。因此,我们得出结论,α-辅肌动蛋白是Z细丝的一种成分,并且无定形基质至少由这些Mr 75,000和55,000的蛋白质组成。