Subcellular distribution and activities of superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase in the southern armyworm, <i>Spodoptera eridania</i>

Abstract

Abstract In mid‐fifth‐instar larvae of the southern armyworm, Spodoptera eridania , the subcellular distribution of four antioxidant enzymes—superoxide dismutase (SOD), catalase (CAT), glutathione peroxidase (GPOX), and glutathione reductase (GR)—were examined. Two‐thirds (4.26 units ·mg protein −1 ) of the SOD activity was found in the cytosol, and one‐thirds (2.13 units ·mg protein −1 ) in the mitochondria. CAT activity was unusually high and not restricted to the microsomal fraction where peroxisomes are usually isolated. The activity was distributed as follows: cytosol (163 units) mitochondria (125 units) and microsomes (119 units). Similar to CAT, the subcellular compartmentalization of both GPOX and GR was unusual. No activity was detected in the cytosol, but in mitochondria and microsomes, GR levels were 5.49 and 3.09 units. Although GPOX activity exhibited 14–16‐fold enrichment in mitochondria and microsomes, respectively, over the 850g crude homogenate, the level was negligible (mitochondria = 1.4 × 10 −3 units; microsomes = 1.6 × 10 −3 units), indicating that this enzyme is absent. The unusual distribution of CAT has apparently evolved as an evolutionary answer to the absence of GR from the cytosol, and the lack of GPOX activity.