| pubmed-article:7441301 | pubmed:abstractText | Microtubules were shown to remain intact in brain slices and subfractions maintained at 0 degrees C for 1 h. Under the same conditions, microtubules isolated from brain by warm assembly-cold disassembly methods, disassemble into their constituent subunit proteins. No selective depletions of microtubules were seen when brain slices were incubated in homogenizing buffer at either 0 degrees C or 37 degrees C. The response of native microtubules in brain slices in incubation in other solutions showed that their properties were otherwise the same as those of assembled microtubules. The separated alpha and beta subunits of isolated cold labile and cold stable microtubules were compared by electrophoresis and isoelectric focusing and were shown to possess the same mobilities. The results suggest that native microtubules are temperature insensitive and that isolated microtubules are assembled from pre-existing pools of subunit proteins. The results further suggest that native microtubules possess a factor, lacking in isolated assembled microtubules, which confers temperature stability on the former. | lld:pubmed |
