Ashby B, Frieden C, Bischoff R
J Cell Biol. 1979 May;81(2):361-73. doi: 10.1083/jcb.81.2.361.
Fluorescent antibody staining experiments with both isolated myofibrils and muscle fibers grown in culture show that AMP deaminase is bound to the myofibril in the A band. The strongest staining occurs at each end of the A band. The approximate width of the fluorescent stripes and their relation to the A band remains constant as a function of sarcomere length. Removal of enzyme from the myofibrils leads to loss of staining, and readdition of purified enzyme restores the original staining pattern. A histoenzymatic method for the detection of AMP deaminase activity in cultured fibers gives comparable localization. The results are consistent with the previous observation (Ashby, B. and C. Frieden. 1977.J. Biol. Chem. 252:1869--1872) that AMP deaminase forms a tight complex in solution with subfragment-2 (S-2) of myosin or with heavy meromyosin (HMM).
对分离出的肌原纤维和在培养中生长的肌纤维进行的荧光抗体染色实验表明，AMP脱氨酶结合在A带的肌原纤维上。最强的染色出现在A带的两端。荧光条纹的大致宽度及其与A带的关系随肌节长度的变化保持恒定。从肌原纤维中去除酶会导致染色消失，重新添加纯化的酶可恢复原来的染色模式。一种用于检测培养纤维中AMP脱氨酶活性的组织酶学方法给出了类似的定位结果。这些结果与之前的观察结果（阿什比，B.和C.弗里登。1977年。《生物化学杂志》252:1869 - 1872）一致，即AMP脱氨酶在溶液中与肌球蛋白的亚片段2（S - 2）或重酶解肌球蛋白（HMM）形成紧密复合物。
