Arner A
Pflugers Arch. 1982 Dec;395(4):277-84. doi: 10.1007/BF00580790.
Strips of intact and chemically skinned (Triton X-100) taenia coli were mounted for isometric and quick-release experiments at 23 degrees C. Active force increased in repeated high-K+ induced contractures in the intact muscle. Stable maximal force was 313 +/- 24 mN/mm2 (n = 6). The skinned preparations activated by Ca2+, at 2 mM Mg2+, 3.2 mM MgATP and ionic strength 0.085 M, gave half maximal force at pCa = 5.62 +/- 0.4 and a maximal force (63 +/- 8 mN/mm2) at pCa = 4.5 (20-25% of the control K+-responses prior to skinning but about 60% of the first K+-response). Force-velocity relations were obtained from intact muscles and from the same muscles chemically skinned and activated at optimal Ca2+. Maximal shortening velocity (Vmax) was unaltered in the skinned preparation compared to the intact muscle (0.138 +/- 0.011 vs 0.140 +/- 0.006 L/s) indicating similar kinetics of actomyosin interaction. In the intact muscle a decrease in Vmax was found when the Ca2+ concentration was reduced. Calmodulin (1 microM) increased Ca2+ sensitivity (by about 0.6 log units) of the skinned preparation but at optimal Ca2+ caused no alteration in isometric force or Vmax.
将完整的和经化学去膜(Triton X - 100)处理的结肠带条在23℃下安装用于等长和快速释放实验。在完整肌肉中,重复的高钾诱导挛缩时主动力增加。稳定的最大力为313±24 mN/mm²(n = 6)。在2 mM Mg²⁺、3.2 mM MgATP和离子强度0.085 M条件下,经Ca²⁺激活的去膜制剂在pCa = 5.62±0.4时产生半数最大力,在pCa = 4.5时产生最大力(63±8 mN/mm²)(去膜前对照钾反应的20 - 25%,但约为首次钾反应的60%)。从完整肌肉以及经化学去膜并在最佳Ca²⁺条件下激活的同一肌肉获得力 - 速度关系。与完整肌肉相比,去膜制剂中的最大缩短速度(Vmax)未改变(0.138±0.011对0.140±0.006 L/s),表明肌动球蛋白相互作用的动力学相似。在完整肌肉中,当Ca²⁺浓度降低时,Vmax降低。钙调蛋白(1 μM)增加了去膜制剂的Ca²⁺敏感性(约0.6个对数单位),但在最佳Ca²⁺条件下对等长力或Vmax无影响。