Insect glutathione S-transferase: Separation of transferases from fat bodies of American cockroaches active on organophosphorus triesters

Variability in acetylcholinesterase and glutathione S‐transferase activities in Chironomus riparius meigen deployed in situ at uncontaminated field sites

“…Glutathione S ‐transferase is induced by both organophosphate and organochlorine insecticides in the housefly [9,35] and the American cockroach [7]; it is induced in the bulb mite Rizoglyphus robini by phenobarbital and insecticides [36], and phenobarbital also produced about a threefold induction in the house fly [37]. However, it remains unclear to what extent an induction in GST activity can be expected in C. riparius exposed in situ to xenobiotics, so the ability of this biomarker to detect contaminants in the field is open to question.…”

“…Glutathione S ‐transferase is a family of detoxicating enzymes that catalyze the conjugation of reduced glutathione with a group of compounds having electrophilic centers. These can include nitrocompounds [7], organophosphates [7,8], and organochlorines [9]. The reduced glutathione conjugation products become less toxic and more water soluble so that they can be easily excreted from cells after further metabolism.…”

Enzymes Involved in the Metabolism of Plant Allelochemicals

“…It also occurs in Malpighian tubules and testes of the southern armyworm . The activities have been found in the tufted apple budmoth, Platynota idaeusalis (Walker) (Lepidoptera: Tortricidae) (Wells et al, 1983), house flies (Ottea and Plapp, 1981;Oppenoorth et al, 1977;Hayaoka and Dauterman, 1983), fruit flies (Jansen et al, 1984), the Mediterranian fruit fly, Ceratitis capitata (Wiedemann) (Diptera: Tephritidae) (Yawetz and Koren, 1984), the migratory locust, Locusta migratoria cinerascens (Orthoptera: Locustidae) (Menguelle et al, 1985), the New Zealand grass grubs, Costelytra zealandica (White) (Coleoptera: Scarabaeidae) (Clark et al, 1985) and the porina moth, Wiseana cervinata (Lepidoptera: Hepialidae) (Clark and Drake, 1984), fatbodies of American cockroaches (Usui et al, 1977), other cockroaches, a flour beetle (Tenebrio), a cotton stainer (Dysdercus), a turnip beetle (Phaedon), and locusts (Schistocerca) (Cohen et al, 1964), the orange tortrix and the braconid Oncophanes americanus , the honey bee (Yu et al, 1984), and adult and larval boll weevils (Brattsten, 1986a). The gluthatione transferases thus occur widely among insects of different orders, with different life styles and in different life stages; they also occur in several different tissues.…”

“…Several other model substrates have been used with insect enzyme preparations including l-chloro-2,4-dinitrobenzene, methyl iodide, butyl iodide, transcinnamaldehyde, 1,2-epoxy-3-(p-nitrophenoxy) propane (Usui et al, 1977;Yu, 1984;Gunderson et al, 1986;Brattsten, 1986a). A distinct advantage in studying the glutatione transferases is their considerable storage stability; post-microsomal supernatants can be stored for many months at _20 0 C without loss in activity.…”

Chemical Self-Defense by Termite Workers: Prevention of Autotoxication in Two Rhinotermitids

“…We had begun this project with the expectation that either mercapturic acids or glutathione conjugates (13,14) would be isolated as the primary detoxication products, in which addition of nucleophilic sulfhydryl groups to the unsaturated systems would provide more water-soluble, less reactive compounds. Glutathione S-transferase activity has been found in flies (15), caterpillars (16), cockroaches (17), and other invertebrates (18), and is implicated in resistance to chloronitrobenzenes, diazinon, and various organophosphorus insecticides (15). Although these two termite species do have glutathione S-transferase activity (8), this is clearly not the primary mode of detoxication.…”