Stabrovskaia V I, Braun A D
Tsitologiia. 1983 Jun;25(6):699-702.
A study was made of solubilization of aldolase isolated from homogenates of skeletal muscles, both intact and being in the state of contracture due to urea action. Compared to water, electrolytes extract more aldolase from homogenates of intact and altered muscles. Almost the same amounts of aldolase were extracted with electrolytes from homogenates of muscles, which lost irreversibly their excitability, and of intact muscles. The actomyosin isolated from muscles displayed aldolase activity not removed under reprecipitation. The aldolase activity of actomyosin, the increase in sorption activity of proteins due to their conformational changes, and the decrease in excitability of aldolase isolated from homogenates of altered muscles by urea doses inducing denaturation of actomyosin and aldolase, all this may suggest that the action of injured agents on muscle stimulates the ability of aldolase and actomyosin to interact. The ratio of free and bound forms of aldolase differs in the intact and in the altered muscle cell.
对从完整骨骼肌匀浆以及因尿素作用而处于挛缩状态的骨骼肌匀浆中分离出的醛缩酶的增溶作用进行了研究。与水相比，电解质能从完整和改变后的肌肉匀浆中提取出更多的醛缩酶。从不可逆丧失兴奋性的肌肉匀浆和完整肌肉匀浆中，用电解质提取出的醛缩酶量几乎相同。从肌肉中分离出的肌动球蛋白表现出在再沉淀时未被去除的醛缩酶活性。肌动球蛋白的醛缩酶活性、蛋白质因构象变化而导致的吸附活性增加，以及用诱导肌动球蛋白和醛缩酶变性的尿素剂量从改变后的肌肉匀浆中分离出的醛缩酶的兴奋性降低，所有这些可能表明损伤因子对肌肉的作用刺激了醛缩酶和肌动球蛋白相互作用的能力。完整和改变后的肌肉细胞中醛缩酶的游离形式和结合形式的比例不同。
