Kjörell U, Thornell L E
Eur J Cell Biol. 1982 Aug;28(1):139-44.
A three-dimensional cytoskeleton, morphologically composed of intermediate filaments, desmosomes, and Z-disks, remains in bovine heart Purkinje fibres after extraction with Triton X-100 and low and high ionic strength solutions. Biochemically this cytoskeleton mainly consists of skeletin (Mr approximately 55 000) and of alpha-actinin (Mr approximately 95 000). Minor high molecular weight components are also present. By gel electrophoresis-derived enzyme-linked immunosorbent assay (GEDELISA) we show here that a 150 000-dalton component is a complex of alpha-actinin and skeletin. Furthermore, this 150 000-dalton component has now been purified and can be converted into 95 000- and 55 000-dalton subunits by reduction with a high concentration of beta-mercaptoethanol and heating. We also show that solubilized pure skeletin and pure alpha-ctinin from Purkinje fibres, after mixing, partly form a stable complex with a molecular weight of about 150 000 daltons.
一种三维细胞骨架，形态上由中间丝、桥粒和Z盘组成，在用 Triton X - 100以及低离子强度和高离子强度溶液提取后，仍存在于牛心脏浦肯野纤维中。从生化角度来看，这种细胞骨架主要由骨骼蛋白（分子量约为55000）和α - 辅肌动蛋白（分子量约为95000）组成。也存在少量高分子量成分。通过凝胶电泳衍生的酶联免疫吸附测定（GEDELISA），我们在此表明一种150000道尔顿的成分是α - 辅肌动蛋白和骨骼蛋白的复合物。此外，这种150000道尔顿的成分现已被纯化，通过用高浓度的β - 巯基乙醇还原并加热，可以转化为95000道尔顿和55000道尔顿的亚基。我们还表明，从浦肯野纤维中溶解的纯骨骼蛋白和纯α - 辅肌动蛋白混合后，部分形成了一种分子量约为150000道尔顿的稳定复合物。
