Purification and characterization of sheep brain cold-stable microtubules.
Purification and characterization of sheep brain cold-stable microtubules.
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羊脑冷稳定微管的纯化和表征。
DOI：
10.1073/pnas.80.6.1560
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发表时间：
1983
影响因子：
11.1
通讯作者：
Margolis,RL
中科院分区：
文献类型：
--
作者：
Pirollet,F;Job,D;Fischer,EH;Margolis,RL
高产量冷稳定微管的分离，以前只描述从啮齿动物，扩展到高等动物的大脑。在最佳条件下，每100 g羊脑可获得30 mg冷稳定微管的常规产量。通过两个聚合循环纯化的材料显示出与从大鼠获得的纯化材料相同的对低温或钙的千摩尔浓度的稳定性，以及对钙调素和ATP的稳定性[Job， D., Rauch， C.T., Fischer， E.H. & Margolis， R.L. (1982) Biochemistry 21,509]。此外，DE-52色谱的这种材料产生的部分，恢复冷稳定性，当添加到冷不稳定的微管。已知与钙调素结合并增强微管组装的tau蛋白没有冷稳定活性。羊脑和大鼠脑冷稳定部分的蛋白谱相似，但没有显示与tau蛋白对应的蛋白带。
The isolation of cold-stable microtubules in high yields, described previously only from rodents, was extended to the brain of higher animals. Under optimal conditions, yields of 30 mg of cold-stable microtubles per 100 g of sheep brain could be obtained routinely. Material purified by two polymerization cycles displayed the same stability to cold temperature or to millimolar concentrations of calcium and the same lability to calmodulin and to ATP as did the purified material obtained from the rat [Job, D., Rauch, C.T., Fischer, E.H. & Margolis, R.L. (1982) Biochemistry 21, 509]. Furthermore, DE-52 chromatography of this material yielded a fraction that restored cold stability when added to cold-labile microtubules. Known to bind to calmodulin and to enhance microtubule assembly, tau proteins had no cold-stabilizing activity. Protein profiles of the cold-stabilizing fraction from sheep and rat brain were similar to one another but showed no protein bands corresponding to the tau proteins.