ANTIOXIDANT ENZYME-ACTIVITIES IN SUBCELLULAR-FRACTIONS OF LARVAE OF THE BLACK SWALLOWTAIL BUTTERFLY, PAPILIO-POLYXENES

The black swallowtail butterfly, Papilio polyxenes, larvae are specialized feeders of pro‐oxidant rich plants of Apiaceae and Rutaceae. An important defense against toxic forms of oxygen species generated by ingestion of the pro‐oxidants, are the antioxidant enzymes, superoxide dismutase (SOD), catalase (CAT), GSH‐dependent glutathione peroxidases (selenium‐dependent glutathione peroxidase [GPOX] and peroxidase activity of selenium‐independent glutathione‐S‐transferase [GTpx]), and glutathione reductase (GR). The subcellular distribution of these enzymes in black swallowtail larvae was investigated and was found to resemble the patterns described for larvae of two other lepidopteran species: the southern armyworm, Spodoptera eridania, and the cabbage looper, Trichoplusia ni. The confinement of SOD in the cytosol and mitochondria was typically eukaryotic, but the relative proportion (1:1) was markedly different from the mammalian pattern (4:1; cytosol:mitochondria). The most obvious difference between the black swallowtail and other lepidoptera as a group, and mammalian species, is in very wide intracellular distributions of CAT, GTpx, and GR in insect species. Insects possess very low levels of a GPOX‐like activity which reduces both H2O2 and organic peroxides. Consequently, insects have elaborate activities with a wide subcellular distribution of both CAT which decomposes H2O2, and GTpx which decomposes organic peroxides. The reduction of peroxides is dependent on GSH, which in this process is oxidized to GSSG. GR which reduces GSSG to GSH is also of wide subcellular distribution, analogous to the distribution pattern of GTpx. Copyright © 1990 Wiley‐Liss, Inc.