基因重组人类神经Tau溶液结构与功能研究

The recombinant human neuronal tau-40 is expressed and purified before its structure and function during denaturation and renaturation are studied by analyses of fluorescence, ultraviolet, light-scattering, enzymic cleavage (earthworm fibrinolytic enzyme) and other methods. The results show that neuronal tau is partially to possess a relative stable conformation in solutions, suggesting a fast kinetic renaturation of tau from thermal denaturation, but not like "a native dentured state" at room temperature. A new fluorophore could form (Ex 230, 280 nm and Em 333nm) when tau incubated in solutions, such as phosphate and Tris buffers, at either 25°C or 37°C and it could be used as a fluorescent probe to monitor conformational changes of tau molecules. Experiments on interaction of neuronal tau with D-glyeraldehyde-3-phosphate dehydrogenase indicate that tau acts in an anti-chaperon-like manner to the enzyme during denaturation and renaturation. It appears that neuronal tau can interact with some important proteins aside from its assemblying and stabilizing the microtubule system.

Tau蛋白具有促进微管装配和稳定微管系统的作用，是老年性痴呆等疾病患者大脑内神经纤岬闹饕煞帧１究翁饽庋∮梦⒐艿鞍缀?-磷酸甘油醛脱氢酶为底物研究tau蛋白具有分子伴侣的新功能，同时应用荧光、CD、紫外差光谱及化学修饰等技术研究该蛋白在变形与复性过程中的结构特性。