Reichsman F, Scordilis S P, Clarkson P M, Evans W J
University of Massachusetts, Amherst.
Eur J Appl Physiol Occup Physiol. 1991;62(4):245-50. doi: 10.1007/BF00571547.
This study characterized changes in the protein composition of human muscle tissue after eccentric exercise. Four subjects performed 70 maximum eccentric, isokinetic actions of the forearm flexors with one arm. The other arm served as control. A biopsy of the biceps muscle of each arm was taken 2 days after exercise when muscles were very sore (mean = 8.0; 1 = normal; 10 = very, very sore), and muscle damage was documented by a mean decrease of 0.2 radians in the relaxed elbow angle. Proteins from the biopsy tissue were solubilized in a high ionic strength buffer containing several proteolytic inhibitors. Protein concentrations of the extracts were determined and identical amounts loaded onto sodium dodecyl sulfate (SDS) polyacrylamide gels (7.5, 12.5, and 17.5%). Densitometric analysis of the Coomassie brilliant blue stained gels revealed alterations in the amounts of three protein bands in the exercised tissue relative to the control. These changes were in the linear portion of the graph of absorbance versus protein amount. Wilcoxon's signed rank test showed the first two of the following bands to increase significantly in amount (P less than 0.062). The average percentage changes [mean (SEM)] for these bands were 63 (21), 39 (5), and 82 (35). The corresponding molecular weights determined from known standards were 76300 (860), 33200 (310), and 12000 (80) daltons, respectively. These changes imply that the increased synthesis, decreased degradation, or some combination thereof, of these three proteins may be necessary for the repair or regeneration response to exercise-induced muscle damage.
本研究对离心运动后人肌肉组织的蛋白质组成变化进行了表征。四名受试者用一只手臂进行了70次前臂屈肌的最大离心等速动作。另一只手臂作为对照。在运动后2天,当肌肉非常酸痛时(平均=8.0;1=正常;10=非常非常酸痛),对每只手臂的肱二头肌进行活检,并且通过放松肘部角度平均下降0.2弧度记录肌肉损伤。活检组织中的蛋白质溶解在含有几种蛋白水解抑制剂的高离子强度缓冲液中。测定提取物的蛋白质浓度,并将等量的提取物加载到十二烷基硫酸钠(SDS)聚丙烯酰胺凝胶(7.5%、12.5%和17.5%)上。对考马斯亮蓝染色凝胶的光密度分析显示,与对照相比,运动组织中三条蛋白带的量发生了变化。这些变化处于吸光度与蛋白量关系图的线性部分。威尔科克森符号秩检验显示,以下前两条带的量显著增加(P小于0.062)。这些带的平均百分比变化[平均值(标准误)]分别为63(21)、39(5)和82(35)。根据已知标准确定的相应分子量分别为76300(860)、33200(310)和12000(80)道尔顿。这些变化意味着这三种蛋白质的合成增加、降解减少或两者的某种组合可能是运动诱导的肌肉损伤修复或再生反应所必需的。