Donahue M J, Michnoff C A, Masaracchia R A
Comp Biochem Physiol B. 1985;82(2):395-403. doi: 10.1016/0305-0491(85)90259-7.
The regulatory proteins of Ascaris suum striated skeletal muscle were partially purified and characterized. A tropomyosin isoform (Mr 41K) and three troponin subunits identified as troponin T (Mr 37.5K), troponin I (Mr 25.5K) and troponin C (Mr 18.5K) were purified. Three myosin light chains (Mr 25K, 19K, and 17K) were isolated from washed Ascaris actomyosin; the 19K subunit was phosphorylated in vitro. A calcium/calmodulin-dependent myosin light chain kinase activity was identified in the muscle. In contrast to previously reported data suggesting that Ascaris obliquely striated muscle contraction is regulated by a myosin-mediated mechanism, these data indicate that all of the proteins required for actin-mediated, calcium-dependent muscle contraction are present in this tissue.
对猪蛔虫横纹肌的调节蛋白进行了部分纯化和特性鉴定。纯化出一种原肌球蛋白异构体(分子量41K)以及三种肌钙蛋白亚基,分别鉴定为肌钙蛋白T(分子量37.5K)、肌钙蛋白I(分子量25.5K)和肌钙蛋白C(分子量18.5K)。从洗涤后的蛔虫肌动球蛋白中分离出三种肌球蛋白轻链(分子量25K、19K和17K);19K亚基在体外被磷酸化。在肌肉中鉴定出一种钙/钙调蛋白依赖性肌球蛋白轻链激酶活性。与之前报道的数据表明蛔虫斜纹肌收缩受肌球蛋白介导机制调节不同,这些数据表明该组织中存在肌动蛋白介导的、钙依赖性肌肉收缩所需的所有蛋白质。