ワモンゴキブリの解糖作用におよぼす殺線虫剤の影響

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Carbohydrates, crude fat, α-glycerophosphate and lactate, in the male American cockroach poisoned by ethylene dibromide (EDB), 1,2-dibromo-3-chloropropane (DBCP) and cis-1,3-dichloropropene (cis-D), were determined. The roaches poisoned by EDB or monoiodoacetate utilized a small amount of carbohydrates as compared with the untreated insect, but the roaches poisoned by DBCP or cis-D utilized much more carbohydrates than the untreated roach. There was no difference in the utilization of crude fat between the insects poisoned by EDB, DBCP or cis-D and the untreated insect. Lactate accumulated much more in the insects poisoned by potassium cyanide, DBCP or EDB than the untreated insect, but no quantitative difference was observed between the insects poisoned by cis-D or monoiodoacetate and the untreated insect. α-Glycerophosphate accumulated much more in the roaches poisoned by potassium cyanide or cis-D than the untreated insect, but did not accumulate in the insect poisoned by EDB or DBCP. Inhibitory effects of EDB on the enzymes involved in the Embden-Meyerhof sequence were studied, using the preparation extracted from the American cockroach coxae with 0.9 per cent potassium chloride solution. Hexokinase, phosphohexose isomerase, phosphofructokinase, α-glycerophosphate dehydrogenase, aldolase, triosephosphate isomerase, phosphoglucomutase, enolase and lactic dehydrogenase were not inhibited by EDB at a level of 10^<-3>M in vitro. Triosephosphate dehydrogenase was inhibited by EDB both in vitro and in vivo. In vitro inhibition was about 79 per cent at final concentration 10^<-4>M of EDB. In vivo inhibition of triosephosphate dehydrogenase by EDB was parallel to the development of poisoning symptom, and about 58 per cent inhibition of the enzyme was observed at the stage of paralysis of the roach. Therefore, the inhibition toward triosephosphate dehydrogenase might be important for the toxicity of EDB to the cockroach. Triosephosphates, consisted of D-glyceraldehydehyde-3-phosphate and dihydroxyacetone phosphate, accumulated in the poisoned roaches with either EDB or monoiodoacetate, twice as much as in the untreated roach. When the enzyme preparation had been preincubated with a higher concentration of glutathione (GSH) (final concentration of 1.2×10^<-4>M) and EDB for 30 minutes at 0℃, triosephosphate dehydrogenase was inhibited only slightly by EDB, whereas the enzyme was inhibited highly by EDB if the final concentration of GSH was reduced to 1.2×10^<-6>M. When the enzyme activity was determined immediately after the addition of GSH preincubated with EDB for 30 minutes at room temperature, the inhibitory effect of EDB increased accompanying with the rise of EDB concentration, although it was lower than the preincubation of the enzyme with GSH and EDB. Chemical reaction of EDB with GSH may occur, but it seems to be less than the reaction of EDB with triosephosphate dehydrogenase. EDB inhibited the enzyme activity in the presence of GSH, and the inhibition appeared gradually with the incubation time. It is likely that the inhibition was proceeded by the reaction of EDB with SH-group of the enzyme. DBCP and cis-D did not inhibit the activities of triosephosphate dehydrogenase in vitro. Ethylene iodide inhibited the triosephosphate dehydrogenase activity in vitro as like as EDB, while ethylene dichloride did not inhibit the enzyme,
日本応用動物昆虫学会の論文
1964-12-25

ワモンゴキブリの解糖作用におよぼす殺線虫剤の影響

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