Hydrofluoric Acid-treated T ~ H F Proteins Display the Same Biochemical Properties as Normal T*
Hydrofluoric Acid-treated T ~ H F Proteins Display the Same Biochemical Properties as Normal T*
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氢氟酸处理的 T ~ H F 蛋白显示出与正常 T* 相同的生化特性
DOI：
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发表时间：
2001
期刊：
影响因子：
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通讯作者：
Binder
中科院分区：
文献类型：
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作者：
Sharon;Greenberg;Peter Daviesll;Joshua D. Scheinq;Lester;I.;Binder
Tau（7）是阿尔茨海默病中发现的成对螺旋丝（PHF）的主要成分。本研究探讨了PHF相关T蛋白（T~HF）的独特性质是由正常可溶性T（T ~）翻译后修饰引起的可能性。经氢氟酸（HF）处理后，TPHF蛋白质是热和酸稳定的，可溶于24 N-吗啉代）乙磺酸缓冲液，并显示出与正常7相同的分子量、PI和免疫化学性质。碱性磷酸酶处理的游离PHF的结果相似，但不太广泛，电泳的变化和减少PHF-1免疫反应性。因此，正常T.似乎是负责的独特性质的T~HF。虽然我们的结果表明，所有的正常T亚型是在PHF，个别T物种的相对丰度不同HF处理的PHF和T。样品此外，HF治疗后PHF的丢失表明，翻译后修饰有助于PHF的结构稳定性。
Tau (7) is a major constituent of paired helical fila- ments (PHF) found in Alzheimer’s disease. The current study examines the possibility that the distinct prop- erties of PHF-associated T proteins (T~HF) result from post-translational modifications of normal soluble T ( T ~ ) . Following hydrofluoric acid (HF) treatment, TPHF proteins are heat- and acid-stable, soluble in 24N-morpho1ino)ethanesulfonic acid buffers and display the same molecular weight, PI, and immunochemical properties as normal 7.. Alkaline phosphatase treatment of dissociated PHF results in similar, although less extensive, electrophoretic changes and a reduction in PHF-1 immunoreactivity. Therefore, phosphorylation of normal T. appears to be responsible for the distinct properties of T~HF. Although our results suggest that all of the normal T isoforms are in PHF, the relative abun- dance of individual T species differs in HF-treated PHF and T. samples. Moreover, the loss of PHF following HF treatment suggests that post-translational modifications contribute to the structural stability of PHF.