ARTICLE

THE LOCALIZATION OF MYOFIBRILLAR ATPASE ACTIVITY IN THE FLIGHT MUSCLES OF THE BLOWFLY, CALLIPHORA ERYTHROCEPHALA

Lois W. Tice M.D.¹ and David S. Smith Ph.D.¹

¹ From the Department of Pathology, College of Physicians and Surgeons of Columbia University, New York, and the Department of Zoology, Cambridge University, Cambridge, England.

Dr. Tice's present address is National Institutes of Health, Bethesda. Dr. Smith's present address is Department of Biology, University of Virginia, Charlottesville

The distribution of ATPase activity in the asynchronous flight muscles of Calliphora erythrocephala (Diptera) was studied at a fine structural level, using preparations of teased fibers, both unfixed and after brief fixation in hydroxyadipaldehyde, incubated in a medium for the histochemical demonstration of myosin or actomyosin ATPase. In relaxed fibrils, activity was found confined to the A bands and was absent from the H zones as well as from the Z and I band regions. At high magnification, deposits of final product, lead phosphate, appeared primarily related to the thick filaments, or to short lateral extensions from them. Evidence was gathered which indicated that this enzyme activity was that of a triphosphatase which did not act on dinucleoside or non-nucleoside substrates.

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