Pette D, Schnez U
Histochemistry. 1977 Oct 22;54(2):97-107. doi: 10.1007/BF00489668.
Single muscle fibres were isolated by microdissection from freeze-dried samples of rabbit psoas and soleus muscles. The individual fibres were typed according to qualitative histochemical reactions for succinate dehydrogenase or NADH-tetrazolium reductase and for alkaline Ca2+-activated myofibrilla myosin ATPase after acid or alkaline preincubation. Methods are described for electrophoretic analysis by means of polyacrylamide disc electrophoresis in the presence of SDS of total myofibrilla proteins in single fibres after pre-extraction of soluble proteins. Fast-twitch white fibres revealed a myosin light chain pattern characteristic of "fast- type" myosin with three light chains of apparent molecular weights of 22,300 (LC1) 18,400 (LC2) and 16,000 (LC3). Fast-twitch red fibres were indistinguishable in this respect from fast-twist white fibres and showed an identical pattern of myosin light chains. Slow-twitch fibres could be characterized by a myosin light chain pattern typical of myosin of slow-twitch muscles with peptides of the apparent molecular weights of 23,500 (LC1Sa), 23,000 (LC1Sb) and 18,500 (LS2S). Slow-twitch fibres isolated from soleus as well as from psoas muscle were indistinguishable with regard to their myosin light chain patterns, thus suggesting that fibres of the same histochemical type correspond in their myosin light chain patterns irrespective of their origin from different muscles.
通过显微解剖从冻干的兔腰大肌和比目鱼肌样本中分离出单根肌纤维。根据琥珀酸脱氢酶或NADH - 四氮唑还原酶以及酸或碱预孵育后碱性Ca2+激活的肌原纤维肌球蛋白ATP酶的定性组织化学反应对单个纤维进行分型。描述了在预提取可溶性蛋白质后，通过SDS存在下的聚丙烯酰胺圆盘电泳对单根纤维中的总肌原纤维蛋白进行电泳分析的方法。快肌白纤维显示出“快型”肌球蛋白的肌球蛋白轻链模式，其三条轻链的表观分子量分别为22,300（LC1）、18,400（LC2）和16,000（LC3）。快肌红纤维在这方面与快肌白纤维无法区分，并且显示出相同的肌球蛋白轻链模式。慢肌纤维的特征在于慢肌肌球蛋白典型的肌球蛋白轻链模式，其肽段的表观分子量为23,500（LC1Sa）、23,000（LC1Sb）和18,500（LS2S）。从比目鱼肌以及腰大肌分离出的慢肌纤维在肌球蛋白轻链模式方面无法区分，因此表明相同组织化学类型的纤维，无论其来自不同肌肉，其肌球蛋白轻链模式都相对应。
