Srihari T, Wiehrer W, Pette D, Harris B G
Mol Biochem Parasitol. 1981 Jun;3(2):71-82. doi: 10.1016/0166-6851(81)90007-4.
A myofibrillar protein extract has been isolated from the muscle of Ascaris suum. Two-dimensional electrophoresis of this extract revealed that the myosin light chain 1 (ALC1) migrates as 3 components with approximate isoelectric points in the range of 5.3-5.6. The most acidic component of ALC1 appeared to be phosphorylated when the myofibrillar extract was incubated for 10 s with catalytic subunit of cAMP dependent protein kinase and [gamma-32P] ATP. The myosin light chain 2 (ALC2) migrated as a single component in isoelectric focusing with an approximate isoelectric point of 5.5 Actin was resolved into 2 components with identical molecular weight but isoelectric points differing by approximatley 0.2 pH units. A protein was tentatively identified in the myofibrillar extract as tropomyosin. It migrated as a single band with an approximate isoelectric point of 5.0 and a molecular weight of 39 000. None of the troponin components could be identified in the myofibrillar extract. It is postulated that muscle contraction in A. suum muscle could be controlled by phosphorylation of myosin.
已从猪蛔虫肌肉中分离出肌原纤维蛋白提取物。对该提取物进行二维电泳分析表明，肌球蛋白轻链1（ALC1）以3种组分形式迁移，其近似等电点范围为5.3 - 5.6。当肌原纤维提取物与环磷酸腺苷依赖性蛋白激酶催化亚基及[γ-32P]ATP孵育10秒时，ALC1的最酸性组分似乎发生了磷酸化。肌球蛋白轻链2（ALC2）在等电聚焦中以单一成分迁移，近似等电点为5.5。肌动蛋白被解析为2种组分，分子量相同但等电点相差约0.2个pH单位。在肌原纤维提取物中初步鉴定出一种蛋白质为原肌球蛋白。它以单一条带形式迁移，近似等电点为5.0，分子量为39000。在肌原纤维提取物中未鉴定出任何肌钙蛋白组分。据推测，猪蛔虫肌肉中的肌肉收缩可能受肌球蛋白磷酸化控制。
