抄録
The binding of Ca2+ ions and Ca-induced change in the hydration of F-actin were studied by a potentiometric technique using Ca sensitive electrode and sound velocity measurement. F-actin bound larger amounts of Ca2+ ions than lysozyme and ovalbumin. Hydration of both F-actin and ovalbumin decreased with addition of small amounts of Ca2+ ions such as 20 μM, but the decrease of hydration in F-actin was larger than that of ovalbumin. Bound ADP of F-actin was suggested to the cause of this phenomenon.
