Bhan A K, Scheuer J
Am J Physiol. 1975 Apr;228(4):1178-82. doi: 10.1152/ajplegacy.1975.228.4.1178.
Cardiac myosin from rats exercised 90 or 150 min daily for 8 wk was compared with the myosin from the hearts of matched sedentary controls. The Ca++-ATPase activity was increased 17 percent in rats exercised 90 min and 30 percent in rats exercised 150 min daily. In the exercised group 0.18 M KCl increased the myosin ATPase activity by 50 percent but had no effect in the control group. Ethylene glycol activated the Ca++-ATPase in control myosin preparations, but had no significant effect on myosin from conditioned hearts. Heavy meromyosin (HMM) from conditioned hearts had a higher Ca++-ATPase activity than from controls. Fluorescence with 8-anilinonaphthalene sulfonate (ANS) was increased 30 percent in HMM from conditioned hearts. The results suggest that the increased myosin ATPase activity in the hearts of exercised animals may be due to a local conformational change at or near the active site.
将每天运动90或150分钟,持续8周的大鼠的心肌肌球蛋白与相匹配的久坐对照大鼠心脏中的肌球蛋白进行比较。每天运动90分钟的大鼠,其Ca++-ATP酶活性增加了17%,而每天运动150分钟的大鼠增加了30%。在运动组中,0.18M KCl使肌球蛋白ATP酶活性增加了50%,但对对照组没有影响。乙二醇激活了对照肌球蛋白制剂中的Ca++-ATP酶,但对适应性心脏的肌球蛋白没有显著影响。适应性心脏的重酶解肌球蛋白(HMM)比对照的具有更高的Ca++-ATP酶活性。来自适应性心脏的HMM中,用8-苯胺基萘磺酸盐(ANS)检测的荧光增加了30%。结果表明,运动动物心脏中肌球蛋白ATP酶活性的增加可能是由于活性位点处或其附近的局部构象变化所致。