Thorstensson A, Sjödin B, Tesch P, Karlsson J
Acta Physiol Scand. 1977 Feb;99(2):225-9. doi: 10.1111/j.1748-1716.1977.tb10373.x.
The enzyme activities of Mg2+ stimulated ATPase, creatine phosphokinase (CPK), myokinase (MK) and lactate dehydrogenase (LDH) were determined in pooled fast twitch (FT) and slow twitch (ST) human skeletal muscle fibers, dissected out from freeze-dried muscle biopsy material. All enzymes investigated demonstrated higher activities in FT fibres. The ratio in enzyme activity between fibre types was greatest for Mg2+ stimulated ATPase (3:1) and smallest for CPK (1.3:1). In addition, the isozyme patterns of CPK, MK and LDH were studied by means of isoelectric focusing (CPK and MK) and discelectrophoresis (LDH). A difference was observed between fibre types with respect to the isozyme distribution of MK and LDH, whereas the CPK isozyme pattern was similar in both fibre types. These results on separated human FT and ST fibres were essentially in conformity with what has earlier been indicated from experiments on mixed muscle homogenates.
从冻干的肌肉活检材料中分离出快肌（FT）和慢肌（ST）人骨骼肌纤维并混合，测定了镁离子刺激的ATP酶、肌酸磷酸激酶（CPK）、肌激酶（MK）和乳酸脱氢酶（LDH）的酶活性。所有研究的酶在快肌纤维中都表现出较高的活性。纤维类型之间的酶活性比值，镁离子刺激的ATP酶最大（3:1），CPK最小（1.3:1）。此外，通过等电聚焦（CPK和MK）和圆盘电泳（LDH）研究了CPK、MK和LDH的同工酶模式。在MK和LDH的同工酶分布方面，观察到纤维类型之间存在差异，而两种纤维类型中的CPK同工酶模式相似。这些关于分离的人快肌和慢肌纤维的结果与早期在混合肌肉匀浆实验中所表明的基本一致。
