シオミズツボワムシのプロテア-ゼに関する研究-1-粗酵素液中のプロティナ-ゼ活性の性質について

概要

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Acid and alkaline proteinase activities were detected in an ammonium sulfate fraction (50-80%) of crude extracts from the rotifer, Brachionus plicatilis. Some properties of the activities in the fraction were investigated. The optimum pH was obtained at about 4.0 for acid proteinase and at about 8.0 for alkaline one. The optimum temperatures of the acid and the alkaline proteinase were 60 and 50℃, respectively, under the experimental condition. The both proteinase activities were unstable as heated at 60℃ for 10 minutes. The acid proteinase activity was inhibited with 1×10⁻³M of Hg²⁺, Cu²⁺, Ag⁺, I₂, monoiodoacetate and PCMB. The alkaline proteinase activity was inhibited with 1×10⁻³M of Hg²⁺, Cu²⁺, Ag⁺, I₂, NBS, DFP, TLCK and potassium permangate.
長崎大学水産学部の論文
1979-02-00