Raghavan K Vijay
Tata Institute of Fundamental Research, Homi Bhabha Road, 400005, Bombay, India.
Wilehm Roux Arch Dev Biol. 1981 Sep;190(5):297-300. doi: 10.1007/BF00848758.
Electrophoresis of myosin extracts from larvae and adult tissues ofDrosophila melanogaster under non-dissociating conditions indicate that two of the bands seen are myosins. They stain for Ca ATPase activity and when cut and re-run under dissociating conditions are found to contain a myosin heavy chain that co-migrates with rabbit skeletal muscle myosin heavy chain. One of the forms of myosin seen is found primarily in extracts from the leg. The other is common to the adult fibrillar flight muscles and the larval body wall muscles.The electrophoretic evidence for two myosin types is strengthened by the histochemical demonstration of two myofibrillar ATPases on the basis of their lability to acid or alkali preincubation. The myofibrillar ATPase in the leg and the Tergal Depressor of the Trochanter (TDT) are shown to be relatively acid labile and alkali stable. The larval body wall muscles and the adult fibrillar flight muscles have an ATPase which is acid stable and alkali labile. This distribution of the two myofibrillar ATPase coincides with that predicted by electrophoresis of extracts from whole tissue and also locates the two myosins to specific muscle types.
在非解离条件下对黑腹果蝇幼虫和成虫组织的肌球蛋白提取物进行电泳分析，结果表明其中两条可见条带为肌球蛋白。它们具有钙ATP酶活性，当在解离条件下切割并重新电泳时，发现含有一条与兔骨骼肌肌球蛋白重链共迁移的肌球蛋白重链。所观察到的一种肌球蛋白主要存在于腿部提取物中。另一种在成虫的纤维状飞行肌和幼虫的体壁肌中都有。基于两种肌原纤维ATP酶对酸或碱预孵育的敏感性差异，通过组织化学方法进一步证实了两种类型肌球蛋白的存在，从而增强了电泳证据。腿部和转子部背板降肌（TDT）中的肌原纤维ATP酶相对对酸敏感而对碱稳定。幼虫体壁肌和成虫纤维状飞行肌中的ATP酶则对酸稳定而对碱敏感。这两种肌原纤维ATP酶的分布与全组织提取物电泳预测的结果一致，也将这两种肌球蛋白定位到特定的肌肉类型。
