Muhlrad A, Afolayan A
J Mechanochem Cell Motil. 1975;3(2):99-101.
1-5 of the epsilon-amino groups of myosin were trinitrophenylated by 2,4,6-trinitrobenzene sulphonate. The Mg2+-activated ATPase activity was found to increase twenty fold while the K+-activated ATPase was strongly inhibited as a result of this treatment. Myosin was dissociated by urea after trinitrophenylation and its heavy and light chains were isolated. Virtually all the introduced trinitrophenyl groups were found in the heavy chain indicating that the lysyl residues, the modification of which affects the ATPase activity, are located at the heavy core of the myosin molecule.
肌球蛋白的ε-氨基中的1至5个被2,4,6-三硝基苯磺酸盐三硝基苯化。结果发现，这种处理使Mg2+激活的ATP酶活性增加了20倍，而K+激活的ATP酶则受到强烈抑制。三硝基苯化后，肌球蛋白被尿素解离，并分离出其重链和轻链。几乎所有引入的三硝基苯基都存在于重链中，这表明其修饰会影响ATP酶活性的赖氨酰残基位于肌球蛋白分子的重核部位。
