The activity of a number of oxidative enzymes, of phosphorylase and UDPG-transglucosylase was studied by histochemical methods in muscle tissue from Schistocerca gregaria. Flight muscle, M. extensor and M. flexor tibiae were assayed separately. In flight muscle, oxidation of glycerol-l-P predominated; the activity of tricarboxylic acid cycle enzymes was relatively low and LDH activity was almost absent. Conversely, LDH was found to be highly active in the leg muscles. Histochemically active reductase systems revealed a mitochondrial pattern characteristic for each muscle type. This pattern was independent of the nature, of the substrate oxidized. A measure of the endogenous cytochrome c content was provided by the cytochrome oxidase reaction. Both the intensity of enzymatic staining of tissue and the amount of formazan produced by muscle homogenate in dehydrogenase systems in vitro compared favourably with known biochemical and structural patterns of locust muscles. Some properties of the histochemical reductase reaction were studied in vitro, using both total homogenate and cytoplasmic fractions. Tétrazolium was indirectly reduced by insect muscle enzyme; the transfer of hydrogen from substrate to dye indicator was mediated by a quinone reductase. In the histochemical system, glycogen was synthetized from both G-l-P and UDPG. The activities of the two glycogen forming systems were reciprocally distributed in flight and leg muscle.

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