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首页> 外文期刊>Biochemistry >MICROTUBULE-ASSOCIATED PROTEINS AND THE FLEXIBILITY OF MICROTUBULES
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MICROTUBULE-ASSOCIATED PROTEINS AND THE FLEXIBILITY OF MICROTUBULES

机译：微管相关蛋白和微管的灵活性

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Experiments were conducted to learn whether the binding of microtubule-associated proteins (MAPs) to microtubules alters the flexibility of the microtubules. Flexibility was measured in vitro by two established techniques. The first employed measurement of the bending of the microtubule in a flow of buffer; the second involved repeated measurement of random thermal fluctuations in the microtubule's shape. Similar values were obtained from microtubules prepared from purified tubulin and those prepared from microtubule protein containing saturating concentrations of MAPs isolated from bovine brain. When measured by the flow technique at 37 degrees C and pH 6.9, the persistence length of pure tubulin microtubules was found to be 8.4 +/- 2.2 mm and that of MAP-containing microtubules was 9.4 +/- 2.7 mm, not significantly different from each other. When measured by the thermal fluctuation technique under identical conditions, values of 6.2 +/- 0.8 and 6.5 +/- 0.8 mm were obtained, again not significantly different from each other. The results show that the binding of MAPs to native microtubules in vitro has little or no effect on their flexibility. MAP-induced effects on the cytoskeleton observed in vivo are likely to be due to other causes, such as formation of microtubule bundles. [References: 29]
机译：进行实验以了解微管相关蛋白（MAPs）与微管的结合是否改变了微管的柔韧性。通过两种既定技术在体外测量柔韧性。首先采用缓冲液流中微管弯曲的测量方法。第二个涉及重复测量微管形状中的随机热波动。从纯化的微管蛋白制备的微管和由饱和浓度的从牛脑中分离出的MAPs的微管蛋白制备的微管，获得了相似的值。当在37摄氏度和pH 6.9下通过流动技术测量时，发现纯微管蛋白微管的持久长度为8.4 +/- 2.2 mm，含MAP的微管的持久长度为9.4 +/- 2.7 mm，与彼此。当在相同条件下通过热波动技术进行测量时，获得的值分别为6.2 +/- 0.8和6.5 +/- 0.8 mm，两者之间也没有显着差异。结果表明，MAPs与天然微管的体外结合对其柔韧性几乎没有影响。体内观察到的MAP诱导的对细胞骨架的影响可能是由于其他原因引起的，例如微管束的形成。 [参考：29]

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