Separation and characterization of microtubule proteins from calf brain

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Abstract
Electrophoresis of microtubule preparations purified from calf brain by repeated cycles of assembly and disassembly showed that they contain many proteins in addition to .alpha.- and .beta.-tubulin. These additional proteins constituted about 17% of the total material present after 5 cycles of assembly and disassembly. Both 1-dimensional and 2-dimensional electrophoretic techniques were used to characterize them. They could be divided into 2 groups: one that contained proteins which remained in constant quantitative ratio to tubulin during the purification cycles, and one composed of proteins which were removed during purification, although inefficiently. Gel filtration chromatography of cold-depolymerized microtubule preparations yielded a polydisperse fraction of high MW containing most of the non-tubulin proteins. This fraction contained flexible filaments about 100 .ANG. in diameter, similar to those reported by Keats and Hall. These fibers may be neurofilaments, and they may be the major source of the group of inefficiently removed proteins.

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