Fitzsimons R B, Hoh J F
Biochem J. 1981 Jan 1;193(1):229-33. doi: 10.1042/bj1930229.
Human myosin from different skeletal muscles was analysed in a non-denaturing gel system, and the isoenzyme composition correlated with the histochemical composition of the muscle. Two components (SM1 and SM2) were associated with type 1 (slow-twitch) fibres, and three (FM1, FM2 and FM3) with type 2 (fast-twitch) fibres. Light-chain analysis was performed in sodium dodecyl sulphate/polyacrylamide gels. There are three light chains (LCs1a, LCS1b and LCs2) in type 1 fibres, and three (LCf1, LCf2 and LCf3) in type 2 fibres. LCf1 and LCs1b co-migrate in sodium dodecyl sulphate gels. The ratio of LCf3/LCf2 is correlated with the distribution of the individual fast isoenzymes. These results explain apparent discrepancies in the literature concerning the light-chain distribution of human myosin.
在非变性凝胶系统中分析了来自不同骨骼肌的人肌球蛋白，其同工酶组成与肌肉的组织化学组成相关。两种成分（SM1和SM2）与1型（慢肌纤维）纤维相关，三种成分（FM1、FM2和FM3）与2型（快肌纤维）纤维相关。在十二烷基硫酸钠/聚丙烯酰胺凝胶中进行轻链分析。1型纤维中有三种轻链（LCs1a、LCS1b和LCs2），2型纤维中有三种（LCf1、LCf2和LCf3）。LCf1和LCs1b在十二烷基硫酸钠凝胶中迁移率相同。LCf3/LCf2的比率与各个快同工酶的分布相关。这些结果解释了文献中关于人肌球蛋白轻链分布的明显差异。
