游离ATP对海胆精子轴丝和动力蛋白ATP酶的抑制作用。

Inhibition of axoneme and dynein ATPase from sea urchin sperm by free ATP.

作者信息

Hayashi M

出版信息

Biochim Biophys Acta. 1976 Jan 23;422(1):225-30. doi: 10.1016/0005-2744(76)90021-8.

Abstract

Sea urchin sperm flagellar ATPase (EC 3.6.1.3) has magnesium-ATP as an effective substrate and is inhibited by free ATP. The inhibition is prevented by high concentration of KCl or NaCl. 0.4 M KCl extracts 48% of ATPase activity from axoneme. The 0.4 M KCl extract and 0.4 M KCl-treated axoneme are also inhibited by free ATP and this inhibition is reversed by KCl. Dynein purified twice by sucrose density gradient centrifugation is also inhibited by free ATP; this inhibition is also reversed by KCl.

摘要

海胆精子鞭毛ATP酶（EC 3.6.1.3）以镁-ATP作为有效底物，并受到游离ATP的抑制。高浓度的KCl或NaCl可防止这种抑制作用。0.4 M KCl可从轴丝中提取48%的ATP酶活性。0.4 M KCl提取物和经0.4 M KCl处理的轴丝也受到游离ATP的抑制，而这种抑制作用可被KCl逆转。通过蔗糖密度梯度离心纯化两次的动力蛋白也受到游离ATP的抑制；这种抑制作用同样可被KCl逆转。