Yamane A, Hirabayashi T
J Biochem. 1985 May;97(5):1419-28. doi: 10.1093/oxfordjournals.jbchem.a135196.
A comparative study of vertebrate ventricle tropomyosin has been carried out from the viewpoint of molecular evolution. The ventricles containing one-component tropomyosin were generally known, and in this paper those containing two components were also found in 8 species among mammals, reptiles, amphibia, and fish, but not among birds. The two components were concluded to be authentic tropomyosin and not artifacts since they showed lower electrophoretic mobilities in the presence of urea, and they were precipitated at pH 4.5 and bound to F-actin. Studies on cysteine contents and cyanogen bromide cleavage peptide patterns revealed that the characteristics of the two tropomyosin components from pig, turtle, amphibia and carp ventricles varied increasingly in that order from typical alpha- and beta-characteristics as seen in rabbit skeletal muscle tropomyosin. The single component of chicken ventricle tropomyosin showed alpha component characteristics in its electrophoretic mobility and cysteine content, and beta component characteristics in cyanogen bromide cleavage peptide pattern. The two components of carp ventricle tropomyosin seemed to be the most primitive, having two cysteine residues per molecule and a cyanogen bromide cleavage peptide pattern different from those of the two components of rabbit skeletal muscle.
从分子进化的角度对脊椎动物心室原肌球蛋白进行了比较研究。一般认为心室含有单一组分的原肌球蛋白,而在本文中,在哺乳动物、爬行动物、两栖动物和鱼类的8个物种中也发现了含有两种组分的心室,但鸟类中未发现。这两种组分被认为是真正的原肌球蛋白而非人为产物,因为它们在尿素存在下电泳迁移率较低,在pH 4.5时沉淀并与F-肌动蛋白结合。对半胱氨酸含量和溴化氰裂解肽图谱的研究表明,猪、龟、两栖动物和鲤鱼心室的两种原肌球蛋白组分的特征差异越来越大,从兔骨骼肌原肌球蛋白中典型的α和β特征依次变化。鸡心室原肌球蛋白的单一组分在电泳迁移率和半胱氨酸含量上表现出α组分特征,在溴化氰裂解肽图谱上表现出β组分特征。鲤鱼心室原肌球蛋白的两种组分似乎是最原始的,每个分子有两个半胱氨酸残基,其溴化氰裂解肽图谱与兔骨骼肌的两种组分不同。