Whalen R G, Schwartz K, Bouveret P, Sell S M, Gros F
Proc Natl Acad Sci U S A. 1979 Oct;76(10):5197-201. doi: 10.1073/pnas.76.10.5197.
The nature of the myosin heavy chain in embryonic muscle tissue, cultured muscle cells, and several adult muscles was investigated. After denaturation with sodium dodecyl sulfate, purified rat myosins were subjected to partial proteolytic cleavage or immunological analysis using microcomplement fixation. Three types of myosin heavy chains could be demonstrated by both approaches. Whereas adult muscles contain fast- or slow-type myosin heavy chains, embryonic tissue and cultured muscle cells harbor a distinct embryonic form. The existence of this distinct form further characterizes the isozymic transitions of contractile proteins during muscle development.
对胚胎肌肉组织、培养的肌肉细胞和几种成年肌肉中肌球蛋白重链的性质进行了研究。用十二烷基硫酸钠变性后，纯化的大鼠肌球蛋白通过部分蛋白水解切割或使用微量补体固定的免疫分析进行检测。两种方法均能证明存在三种类型的肌球蛋白重链。成年肌肉含有快肌型或慢肌型肌球蛋白重链，而胚胎组织和培养的肌肉细胞则含有一种独特的胚胎形式。这种独特形式的存在进一步表征了肌肉发育过程中收缩蛋白的同工酶转变。
