Houston M E, Lingley M D, Stuart D S, Grange R W
FEBS Lett. 1987 Jul 27;219(2):469-71. doi: 10.1016/0014-5793(87)80274-0.
The phosphate content of the fast (LC2F) and two slow (LC2S and LC2S1) phosphorylatable light chains (P-light chains) in myosin isolated from biopsy samples of rested human vastus lateralis muscle averaged 0.21, 0.28 and 0.25 mol of phosphate per mol of P-light chain, respectively. Following a 10 s maximal contraction, phosphate content was increased by almost 2-fold in the fast and two slow P-light chains. After prolonged, moderate cycling activity phosphate content was only slightly increased in the three P-light chains. These data suggest that, unlike animal skeletal muscle, myosin light chain kinase and phosphatase activities are similar in human fast and slow muscle fibres.
从静息的人类股外侧肌活检样本中分离出的肌球蛋白中的快速（LC2F）和两条慢速（LC2S和LC2S1）可磷酸化轻链（P-轻链）的磷酸盐含量，分别平均为每摩尔P-轻链含0.21、0.28和0.25摩尔磷酸盐。在进行10秒的最大收缩后，快速和两条慢速P-轻链中的磷酸盐含量增加了近2倍。经过长时间的适度循环活动后，三条P-轻链中的磷酸盐含量仅略有增加。这些数据表明，与动物骨骼肌不同，人类快肌纤维和慢肌纤维中的肌球蛋白轻链激酶和磷酸酶活性相似。
