Watanabe K, Sasaki F, Khan M A
Histochemistry. 1978 May 16;55(4):293-305. doi: 10.1007/BF00508797.
The histochemical activities of succinic dehydrogenase (SDH) and Ca++-activated ATPase (pHs 7.4 and 9.4) were studied in the larval tail musculature of Rana japonica, Rana catesbeiana and Rana ornativentris. The ATPase reaction product was detected by both light and electron microscopy. 'Red' and 'white' muscle fibres, as distinguished by SDH, showed high and low Ca++-ATPase reaction, respectively, at pHs 7.4, 9.4 and following preincubation in cold K2-EDTA solution. The ultrastructural investigation of Ca++-ATPase reaction at pH 7.4 by the Ca++-citrophosphate technique demonstrated electron-dense reaction product in association with A, I and 'Z' bands, intermyofibrillar (SR) compartment and the mitochondrial inner chamber. However, Pb++ precipitation technique demonstrated Mg++-activated myosin ATPase activity at pH 9.2 ultrastructurally. The present histochemical data suggest that the anuran larval tail 'red' muscle fibres are possible 'slow,' and emphasize a possible lack of correlation between the speed of contraction with their ATPase activity. Moreover, 'red' muscle fibres of the anuran tai- musculature are not equivalent to 'Type I' fibres of higher chordates.
研究了日本林蛙、牛蛙和饰纹姬蛙幼体尾部肌肉组织中琥珀酸脱氢酶（SDH）和Ca++激活的ATP酶（pH值7.4和9.4）的组织化学活性。通过光学显微镜和电子显微镜检测ATP酶反应产物。经SDH区分的“红”肌纤维和“白”肌纤维，在pH值7.4、9.4以及在冷K2 - EDTA溶液中预孵育后，分别显示出高和低的Ca++ - ATP酶反应。通过Ca++ - 柠檬酸盐技术对pH值7.4时Ca++ - ATP酶反应进行的超微结构研究表明，电子致密反应产物与A带、I带和“Z”带、肌原纤维间（SR）区室以及线粒体内腔相关。然而，Pb++沉淀技术在超微结构上显示了pH值9.2时Mg++激活的肌球蛋白ATP酶活性。目前的组织化学数据表明，无尾类幼体尾部的“红”肌纤维可能是“慢”肌纤维，并强调收缩速度与其ATP酶活性之间可能缺乏相关性。此外，无尾类幼体尾部肌肉组织的“红”肌纤维与高等脊索动物的“I型”纤维并不等同。
