Kirillina V P, Stabrovskaya V I
Institute of Cytology, Academy of Sciences of the USSR, Leningrad.
Gen Physiol Biophys. 1989 Oct;8(5):435-46.
The changes in conformation of F-actin induced by the binding of the glycolytic enzyme lactate dehydrogenase were studied in myosin-free single ghost muscle fibres. The formation of the lactate dehydrogenase-F-actin complex was accompanied by changes in the parameters of intrinsic (tryptophan) and extrinsic (rhodaminyl-phalloin) polarized fluorescence of ghost muscle fibre F-actin. Lactate dehydrogenase stimulated actin-activated Mg2+-ATPase of myosin subfragment 1 by 30%. F-actin of ghost fibres depressed lactate dehydrogenase activity to 20% of the initial values. It is suggested that the energy-providing mechanism is coupled with that of muscle contraction through conformational changes in F-actin.
在无肌球蛋白的单个鬼肌纤维中研究了糖酵解酶乳酸脱氢酶结合诱导的F-肌动蛋白构象变化。乳酸脱氢酶-F-肌动蛋白复合物的形成伴随着鬼肌纤维F-肌动蛋白的内在（色氨酸）和外在（罗丹明-鬼笔环肽）偏振荧光参数的变化。乳酸脱氢酶使肌球蛋白亚片段1的肌动蛋白激活的Mg2 + -ATP酶活性提高了30%。鬼纤维的F-肌动蛋白将乳酸脱氢酶活性降低至初始值的20%。提示能量供应机制通过F-肌动蛋白的构象变化与肌肉收缩机制相偶联。
