Jansson E, Sylvén C
Histochemistry. 1983;78(1):121-4. doi: 10.1007/BF00491118.
Histochemical visualization of myoglobin in a benzidine peroxidase reaction suggests that human skeletal muscle fibres are differentiated into fibres having either high or a low myoglobin content. In the present study myoglobin was quantified in single human muscle fibres after being classified as either type I ("slow-twitch") or type II ("fast twitch"). Samples were obtained from m. quadriceps femoris in 4 healthy untrained male subjects using the needle biopsy technique. After freeze-drying, individual fibres were dissected out and classified as either type I or type II by a myofibrillar ATPase stain. Myoglobin analyses were performed on these single fibres by a radioimmunoassay. The myoglobin concentrations were found to be significantly higher in type I than in type II muscle fibres in all 4 subjects and were, on the average, of the same magnitude as found in larger (mixed muscle) samples. The myoglobin concentration ratio between type I and type II fibres ranged from 1.4 to 1.7.
在联苯胺过氧化物酶反应中对肌红蛋白进行组织化学可视化显示,人类骨骼肌纤维可分化为肌红蛋白含量高或低的纤维。在本研究中,在将单根人类肌纤维分类为I型(“慢肌纤维”)或II型(“快肌纤维”)后,对其肌红蛋白进行了定量分析。使用针吸活检技术从4名未经训练的健康男性受试者的股四头肌获取样本。冻干后,解剖出单根纤维,并通过肌原纤维ATP酶染色将其分类为I型或II型。通过放射免疫分析法对这些单根纤维进行肌红蛋白分析。在所有4名受试者中,发现I型肌纤维中的肌红蛋白浓度显著高于II型肌纤维,并且平均而言,其浓度与在较大(混合肌肉)样本中发现的浓度相同。I型和II型纤维之间的肌红蛋白浓度比在1.4至1.7之间。