蚊幼虫における乳酸脱水素酸素 (LDH) の性状と LDH 阻害物質との関係

概要

論文の詳細を見る
Lactate dehydrogenase (LDH) activity is generally detected by reversible reaction using a combination of a substrate and a coenzyme, that is lactate and NAD (NAD-dependent LDH), or pyruvate and NADH (NADH-dependent LDH). In Anopheles stephensi larvae, NAD-LDH and NADH-LDH activities were high and were easily detected after polyacrylamide gel electrophoresis (PAGE), while in Culex pipiens molestus larvae, NADH-LDH could be detected, but NAD-LDH showed very low activity. According to enzyme histochemical studies, Cx. p. molestus had NAD-LDH at the same localities as An. stephensi did, but its activity was very low. NAD-LDH activity of Cx. p. molestus larvae is, therefore, greatly inhibited by the LDH-inhibitor, which is present in the cytosol of the gastric caeca and midgut, and also in the haemolymph. Among the eight mosquito species examined, LDH-inhibitory activity was highest in the species with low NAD-LDH activity, such as Cx. p. molestus. The LDH-inhibitor was seen to specifically inhibit NAD-LDH activity. Although lactate accumulated in An. stephensi larvae, both NAD-LDH and NADH-LDH were active in this species. While in Cx. p. molestus larvae, although neither lactate nor pyruvate was accumulated, NAD-LDH activity was very low. The LDH-glycolysis could be less active. These results suggested that Cx. p. molestus larvae use some other glycolysis.
日本衛生動物学会の論文
2001-12-15