Swatland H J
Stain Technol. 1979 Sep;54(5):245-9. doi: 10.3109/10520297909110679.
Transverse cryostat sections of skeletal muscle were fixed in a solution containing 1.5% glutaraldehyde and 1.5% sulfosalicylic acid and stained in a solution containing equal volumes of 3% hydrogen peroxide and 50% ethanol saturated with o-tolidine. Myoglobin in the sarcoplasm of muscle fibers was precipitated and stained blue. Applicability of this method to cryostat sections, without glutaraldehyde fixations prior to freezing, allowed the myoglobin content of individual muscle fibers to be correlated with other histochemical characteristics of the same fibers seen in serial sections. In the dark red bovine sternomandibularis muscle, fibers with weak adenosine triphosphatase (ATPase) and strong succinate dehydrogenase (SDH) activity always exhibited strong myoglobin staining. An equal degree of staining was found in many fibers with strong ATPase and intermediate to strong SDH activity. Fibers with strong ATPase and weak SDH activity were less strongly stained than the preceding types.
骨骼肌的横向低温恒温器切片固定在含有1.5%戊二醛和1.5%磺基水杨酸的溶液中，并在含有等体积3%过氧化氢和用邻联甲苯胺饱和的50%乙醇的溶液中染色。肌纤维肌浆中的肌红蛋白沉淀并染成蓝色。该方法适用于低温恒温器切片，在冷冻前无需戊二醛固定，使得单个肌纤维的肌红蛋白含量能够与在连续切片中看到的相同纤维的其他组织化学特征相关联。在深红色的牛胸骨下颌肌中，腺苷三磷酸酶（ATPase）活性弱而琥珀酸脱氢酶（SDH）活性强的纤维总是呈现出强烈的肌红蛋白染色。在许多ATPase活性强且SDH活性中等至强的纤维中发现了同等程度的染色。ATPase活性强而SDH活性弱的纤维染色强度低于前几种类型。
