The polypeptides of isolated brain 10nm filaments and their association with polymerized tubulin.

Brain 10 nm filaments were isolated from bovine, rabbit and rat brains by a modification of an existing procedure. The overall polypeptide composition of these preparations was similar to that previously reported for brain neurofilaments. In addition to the major polypeptide component, which has mol. wt. approx. 50 000, three other polypeptides with chain mol. wts. approx. 210 000, 155 000 and 70 000, which correspond to peripheral-nerve neurofilament polypeptides, were consistently found to be present. The mol. wt.-50 000 species was found to be heterogeneous and may contain a component derived from the mol. wt. 70 000 polypeptide. The three higher-molecular-weight polypeptides did not appear to be obviously homologous or to be homologous with myosin or Myxicola neurofilament polypeptides. These same three higher-molecular-weight components were shown to be identical with the polypeptides probably responsible for the 10 nm filaments formed during the early cycles of the tubulin-purification protocol.