Proteins from disassembled microtubules characterized by oligospecific antisera.
The immunochemical properties of in vitro reassembled microtubules were investigated by immunoelectrophoretic techniques. The tubulin dimer gave no measurable immunochemical response, but the tubulin oligomer, the tau-factor and an antigen of about 135 000 daltons all gave precipitating antibodies. Those four proteins were investigated in reassembled microtubules, in DEAE-cellulose purified tubulin, and after molecular sieve chromatography of disassembled and NaCl-dissociated microtubules. Reconstitution of tubulin oligomer from tubulin dimer and tau-factor was also performed. The presence of a unique antigenic structure on tubulin oligomer which was not found in the dissociated components and the role of this aggregate as a nucleation center or intermediate in the assembly of microtubules is discussed.
D000818:Animals; D001921:Brain / Q000276:immunology; D002848:Chromatography, DEAE-Cellulose; D002850:Chromatography, Gel; D005260:Female; D006023:Glycoproteins / Q000276:immunology*; D007123:Immunoelectrophoresis, Two-Dimensional; D008870:Microtubules / Q000276:immunology* / Q000648:ultrastructure; D008970:Molecular Weight; D009419:Nerve Tissue Proteins / Q000276:immunology; D051381:Rats; D014404:Tubulin / Q000276:immunology* / Q000302:isolation & purification
D006023:Glycoproteins; D009419:Nerve Tissue Proteins; D014404:Tubulin