Hemolymph phenol oxidases in Drosophila melanogaster, Locusta migratoria, and Austropotamobius pallipes.
The early enzyme-mediated reaction sequence in the biosynthesis of melanin from L-tyrosine involves an initial hydroxylation (monophenol oxidase activity, MPO) of the aromatic amino acid precursor to form L-dopa (3,4-dihydroxyphenylalanine), and the ensuing oxidation ( diphenol oxidase activity, DPO) of the resultant diphenol to form dopaquinone. By means of high pressure liquid chromatography with electrochemical detection (HPLC-ED) both phenol oxidase activities were observed in the blood (hemolymph) of two species of insect, third-stage larvae of Drosophila melanogaster and adult Locusta migratoria, and in an adult fresh-water crayfish, Austropotamobius pallipes. These results establish that in each species MPO and DPO can be detected readily without the use of exogenous activators.[1]References
- Hemolymph phenol oxidases in Drosophila melanogaster, Locusta migratoria, and Austropotamobius pallipes. Nappi, A.J., Seymour, J. Biochem. Biophys. Res. Commun. (1991) [Pubmed]
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