Kamimura S, Yano M, Shimizu H
J Biochem. 1985 May;97(5):1509-15. doi: 10.1093/oxfordjournals.jbchem.a135206.
Using sea urchin (Hemicentrotus pulcherimus) sperm flagella, ATP hydrolysis coupled to sliding movement of microtubules was investigated. Flagellar axonemes were pretreated with trypsin and the microtubules induced to slide by addition of ATP (50-1,000 microM) at 0-20 degrees C. Motion-dependent hydrolysis of ATP was observed immediately after the addition of ATP, the rate of which was higher than that of steady state hydrolysis in axonemes without trypsin-treatment, or after complete disintegration. The rate of hydrolysis of ATP divided by the sliding velocity of microtubules reflects the ATP consumption necessary per unit distance of microtubule sliding. This parameter varied according to the experimental conditions in that it increased when the ATP concentration or temperature was decreased. Our results suggest that there is not a strict stoichiometric relationship between ATP hydrolysis and sliding distance in the dynein-tubulin system, indicating that the mechanochemical coupling is different from that in beating axonemes.
利用海胆（Hemicentrotus pulcherimus）精子鞭毛，研究了与微管滑动运动偶联的ATP水解。鞭毛轴丝用胰蛋白酶预处理，在0-20℃下通过添加ATP（50-1000 microM）诱导微管滑动。添加ATP后立即观察到依赖运动的ATP水解，其速率高于未用胰蛋白酶处理的轴丝或完全解体后的稳态水解速率。ATP水解速率除以微管滑动速度反映了微管滑动每单位距离所需的ATP消耗。该参数根据实验条件而变化，当ATP浓度或温度降低时它会增加。我们的结果表明，在动力蛋白-微管蛋白系统中，ATP水解与滑动距离之间不存在严格的化学计量关系，这表明机械化学偶联与摆动轴丝中的不同。
