Tanaka M, Tanaka H
J Biochem. 1979 Feb;85(2):535-40. doi: 10.1093/oxfordjournals.jbchem.a132361.
A method for the almost complete extraction of myosin from smooth muscle fibers of the anterior byssal retractor muscle (ABRM) of Mytilus edulis was developed, and functional reformation of thick filaments in the fibers was achieved. Complete removal of myosin from the glycerol-extracted ABRM fibers with a solution containing 600 mM KCl, 5 mM MgCl2, and 5 mM ATP was difficult. However, successive treatments of the ABRM fibers with glycerol and saponin made the plasma membrane permeable to Mg-ATP and myosin. The extraction of myosin completely eliminated the tension induced by the addition of Mg-ATP. Partial recovery of tension development was observed by irrigation of myosin into fibers from which myosin had been extracted. Similar results were obtained using rabbit myosin instead of ABRM myosin. Addition of heavy meromyosin, on the other hand, had a suppressive effect on the tension development, as is the case in glycerinated rabbit psoas muscle fibers.
开发了一种从贻贝前足丝牵缩肌（ABRM）的平滑肌纤维中几乎完全提取肌球蛋白的方法，并实现了纤维中粗肌丝的功能重塑。用含有600 mM KCl、5 mM MgCl2和5 mM ATP的溶液从甘油提取的ABRM纤维中完全去除肌球蛋白是困难的。然而，用甘油和皂素对ABRM纤维进行连续处理使质膜对Mg-ATP和肌球蛋白具有通透性。肌球蛋白的提取完全消除了添加Mg-ATP所诱导的张力。通过将肌球蛋白灌注入已提取肌球蛋白的纤维中，观察到张力发展的部分恢复。使用兔肌球蛋白代替ABRM肌球蛋白也获得了类似的结果。另一方面，添加重酶解肌球蛋白对张力发展具有抑制作用，这与甘油处理的兔腰大肌纤维的情况相同。
