Davydov A A, Sycheva G F, Zborovskiĭ A B
Vopr Med Khim. 1981 May-Jun;27(3):330-4.
Tropomyosin was isolated from human heart and skeletal muscles, liver, kidney and lung tissues. The subunit composition and relative molecular mass of tropomyosins were studied using polyacrylamide gel electrophoresis in presence of sodium dodecylsulfate. The tropomyosin from heart muscle migrated as a homogenous zone and had a relative molecular mass of 34,000 daltons. The tropomyosin from skeletal muscles was separated into two zones containing polypeptides of 47,200 and 35,000 daltons. Proteins from nonmuscular tissues constituted two fractions with relative molecular mass of 35,000 and 29,000 daltons. alpha-Chains of tropomyosins in various human tissues were similar to each other as shown using immunodiffusion procedure.
原肌球蛋白是从人的心脏、骨骼肌、肝脏、肾脏和肺组织中分离出来的。在十二烷基硫酸钠存在的情况下,使用聚丙烯酰胺凝胶电泳研究了原肌球蛋白的亚基组成和相对分子质量。心肌中的原肌球蛋白迁移为一个均匀区,相对分子质量为34,000道尔顿。骨骼肌中的原肌球蛋白被分离成两个区,分别含有47,200和35,000道尔顿的多肽。来自非肌肉组织的蛋白质构成了两个相对分子质量分别为35,000和29,000道尔顿的组分。使用免疫扩散法显示,不同人体组织中原肌球蛋白的α链彼此相似。