自活性線虫(Panagrellus redivivus GOODEY)における三炭糖燐酸脱水素酵素活性とEDBによる阻害について

概要

論文の詳細を見る
The activity of triosephosphate dehydrogenase in Panagrellus redivivus GOODEY and its inhibition by EDB were measured. It was shown that the optimum pH of this enzyme was at 5.3 approximately. The initial rate of reaction in the optimum pH was linear. Following time elapse, there was gradual establishment of an equilibrium. When the amount of enzyme protein ranged from 1 to 4 mg albumin equivalent, the activity was proportional to the amount of protein. Triosephosphate dehydrogenase in P. redivivus was inhibited by EDB either in vitro or in vivo. In vitro inhibition of the enzyme by various molar concentrations of EDB was very similar to the result obtained for the American cockroach, and In-50 value neighboured to 10^<-5>M in both cases. The mortality of P. redivivus by treatment with EDB was closely paralleled with the inhibition of triosephosphate dehydrogenase.
日本応用動物昆虫学会の論文
1965-09-25