Próchniewicz E
Biochim Biophys Acta. 1979 Aug 28;579(2):346-58. doi: 10.1016/0005-2795(79)90062-x.
Crosslinking of F-actin by a bifunctional reagent glutaraldehyde resulted in a marked decrease of viscosity and length of F-actin filaments. The extent and rate of superprecipitation of actomyosin reconstituted from the modified actin were lower than those of unmodified actin-myosin complex, but activation of heavy meromyosin ATPase by the crosslinked actin was higher than by unmodified one. Heavy meromyosin ATPase activated by the crosslinked actin was distinctly less dependent on KCl concentration than that activated by unmodified actin. Turbidity of the modified acto-heavy meromyosin in the presence of ATP exceeded the sum of turbidities of actin and heavy meromyosin, whereas in the case of unmodified acto-heavy meromyosin the turbidity was comparable to that for noninteracting system. The difference in activation of heavy meromyosin. ATPase by the cross-linked and unmodified actin, clearly seen at room temperature, significantly diminished when temperature was lowered to 0 degrees C.
双功能试剂戊二醛使F-肌动蛋白交联，导致F-肌动蛋白丝的粘度和长度显著降低。由修饰后的肌动蛋白重构的肌动球蛋白的超沉淀程度和速率低于未修饰的肌动蛋白-肌球蛋白复合物，但交联肌动蛋白对重酶解肌球蛋白ATP酶的激活作用高于未修饰的肌动蛋白。交联肌动蛋白激活的重酶解肌球蛋白ATP酶对KCl浓度的依赖性明显低于未修饰肌动蛋白激活的重酶解肌球蛋白ATP酶。在ATP存在下，修饰后的肌动蛋白-重酶解肌球蛋白的浊度超过了肌动蛋白和重酶解肌球蛋白浊度之和，而对于未修饰的肌动蛋白-重酶解肌球蛋白，其浊度与非相互作用体系的浊度相当。重酶解肌球蛋白ATP酶被交联和未修饰的肌动蛋白激活的差异在室温下清晰可见，当温度降至0℃时显著减小。
