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- W2000923352 abstract "Abstract Radiometric and spectrophotometric studies were made of larval phenol oxidase activity in the sex-linked recessive, temperature-sensitive, lethal mutant Tum 1 (1, 34.5) of Drosophila melanogaster during formation of melanotic tumors. At the tumor-expressive temperature of 29°C, virtually no phenol oxidase (monophenol or diphenol oxidase) was detected in either the hemolymph or hemocytes of hemizygous (male) Tum 1 larvae during early (72 hr) and late stages (96 and 120 hr) of melanotic tumor formation. Compared to normal Basc, heterozygous (female) Tum 1 showed reduced hemolymph and hemocyte enzyme activities during the two developmental stages studied (96 and 120 hr). At 120 hr, when melanotic tumors were completely manifested in female Tum 1 , total hemolymph monophenol oxidase activity in this mutant was 50% that of Basc and hemolymph diphenol oxidase activity approximately 40% of the activity of Basc hemolymph with three enzyme substrates tested (dopa, dopamine, and N -acetyldopamine). Hemocyte diphenol oxidase activity in female Tum 1 at this stage of development also was comparably reduced to approximately intermediate levels (59% of the activity found in Basc cells), but hemocyte monophenol oxidase activity was substantially lower than the controls (25% of the activity of Basc ). These results suggest that monophenol and diphenol oxidase activities in the Tum 1 mutant are regulated either by the mutant locus itself, or by linked modifiers also on the X chromosome. The progressive reduction in enzyme activity during melanotic tumor formation may result from product inhibition, the sequestering of enzyme-melanoprotein complexes within the pigmented masses, or the depletion of requisite enzyme activators or substrates." @default.
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- W2000923352 date "1988-09-01" @default.
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- W2000923352 title "Phenol oxidase activity during melanotic tumor formation in Drosophila melanogaster" @default.
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- W2000923352 doi "https://doi.org/10.1016/0022-2011(88)90136-x" @default.
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