Evidence for myosin heterogeneity in Drosophila melanogaster

Vijay Raghavan, K. (1981) Evidence for myosin heterogeneity in Drosophila melanogaster Development Genes and Evolution, 190 (5). pp. 297-300. ISSN 0949-944X

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Official URL: http://www.springerlink.com/content/m8221l19178156...

Related URL: http://dx.doi.org/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 Ca2+ 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.

Item Type:Article
Source:Copyright of this article belongs to Springer.
Keywords:Myosins; Drosophila; Muscle
ID Code:58623
Deposited On:31 Aug 2011 11:57
Last Modified:31 Aug 2011 11:57

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