Paulin-Levasseur M, Gicquaud C
Eur J Cell Biol. 1981 Dec;26(1):144-9.
The effect of phalloidin on ultrastructural components involved in movement have been studied in spread cytoplasmic preparations of Amoeba proteus. In absence of phalloidin, actin filaments are usually rare and only myosin rods are observed. With concentrations of phalloidin between 2 X 10(-6) M and 5 X 10(-6) M, numerous F-actin filaments are present in the preparations. Most of these actin filaments are straight, however some appeared branched and interconnected. Higher concentrations of phalloidin inhibit the movement of naked cytoplasm. Fibrils composed by aggregation of F-actin filaments are present in these preparations. Myosin rods are unaffected by phalloidin.
已在变形虫伸展的细胞质制剂中研究了鬼笔环肽对参与运动的超微结构成分的影响。在没有鬼笔环肽的情况下,肌动蛋白丝通常很少见,仅观察到肌球蛋白杆。当鬼笔环肽浓度在2×10⁻⁶ M至5×10⁻⁶ M之间时,制剂中存在大量F-肌动蛋白丝。这些肌动蛋白丝大多是直的,但有些呈现分支并相互连接。更高浓度的鬼笔环肽会抑制裸露细胞质的运动。在这些制剂中存在由F-肌动蛋白丝聚集形成的纤维。肌球蛋白杆不受鬼笔环肽影响。