Fitzsimons R B, Hoh J F
J Neurol Sci. 1981 Nov-Dec;52(2-3):367-84. doi: 10.1016/0022-510x(81)90018-6.
Recently described techniques for separating myosin isoenzymes have been adapted for analysis of myosins from diseased and developing human skeletal muscle. The method is highly suitable for analysis of human myosins because only 2 - 3 mg of muscle are required for routine analyses. Human embryonic/foetal myosins are electrophoretically distinct from mature skeletal myosins, and are not normally detected beyond the first month of post-natal life, except in premature infants. They have a high alkaline calcium-activated ATPase activity. This would account for the histochemical classification of foetal fibres as "Type II", although physiological differences between adult fast-twitch muscle and foetal muscle are well recognized. Foetal myosins are also synthesized in human skeletal muscle under certain pathological circumstances. Their presence in Duchenne dystrophy probably reflects the associated marked muscle regeneration, with immaturity of some muscle cells. The large amounts of foetal myosin present in many cases of infantile spinal muscular atrophy is evidence that innervation is necessary for the normal cessation of foetal myosin synthesis.
最近描述的分离肌球蛋白同工酶的技术已被应用于分析患病和发育中的人类骨骼肌中的肌球蛋白。该方法非常适合分析人类肌球蛋白，因为常规分析仅需2至3毫克肌肉。人类胚胎/胎儿肌球蛋白在电泳上与成熟骨骼肌肌球蛋白不同，除早产儿外，通常在出生后第一个月后就检测不到了。它们具有高碱性钙激活ATP酶活性。这可以解释胎儿纤维在组织化学上被分类为“II型”，尽管成人快肌和胎儿肌肉之间的生理差异已得到充分认识。胎儿肌球蛋白也在某些病理情况下在人类骨骼肌中合成。它们在杜兴氏肌营养不良症中的存在可能反映了相关的明显肌肉再生，以及一些肌肉细胞的不成熟。许多婴儿型脊髓性肌萎缩症病例中存在大量胎儿肌球蛋白，这证明神经支配对于胎儿肌球蛋白合成的正常停止是必要的。
