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Studies on Poly- and Metaphosphatase in Sweetpotato
Get PDFサツマイモ水抽出液を酵素液として用い,ピロ,トリポリおよびトリメタりん酸の酵素的分解について調べた。(1)各硫安の分画には,いずれも,ピロ,トリポリおよびトリメタりん酸分解酵素が含まれており,特にトリメタりん酸分解酵素は,硫安飽和度の高い分画ほど酵素活性が高くなる。(2)至適pHは,ピロ,トリポリおよびトリメタりん酸分解酵素では,いずれもpH4付近にあり,ピロ,トリポリりん酸分解酵素には,pH6～8にも至適pHが認められた。本研究を行なうにあたり,御懇切な御指導をいただいた,本学北里寅男教授ならびに種々の御助言をいただいた桑野安子講師に対し心から感謝する。Among the condensed phosphates, there are polyphosphate and metaphosphate which are distributed widely in the biological world. The enzymes which can hydrolize the above mentioned phosphates also exist in a wide range in higher animals, the leaves of higher plants, molds and bacteriums etc. Having found a rather high degree of enzyme activitties in Sweetpotato, the reporter attempts to point out some characterisic features of there enzyme through the experiments performed. 1. In each fraction with ammonium sulphate, there are pyro-, tripoly- and trimetaphoshatase. Moreover, the trimeta- phosphatase activity becomes higher in accordance with the saturation concentration with ammonium sulphate. 2. Each reaction optimum pH of pyro-, tripoly- and trimeta- phosphatase is about 4. And the reaction optimum pH of pyro- and tripolyphosphatase is 6-8.departmental bulletin pape
Studies on Poly- and Metaphosphatase (Part 3): Effect of Cu^<2+> and Mn^<2+> on Poly- and Metaphosphatase in Potato
Get PDF1.ある条件下では,Mn^およびCu^によって基質が沈澱することが明らかとなった。2.基質が沈澱しない条件下での酵素反応に及ぼすMn^およびCu^の影響を調べた結果Cu^は酵素を阻害するが,Mn^はほとんど阻害せず,アルカリ側ではむしろ活性化する傾向が認められた。3.Cuによるピロりん酸の酵素的分解の抑止は,Cu^によるピロホスファターゼの阻害と基質ピロりん酸の沈澱の両作用によるものであり,Mnによる抑止作用は,基質ピロりん酸を沈澱させ,反応系から除くことに由来するためと結論される。本研究をおこなうにあたり,御懇切な御指導を頂いた本学教授北里寅男先生に,心から感謝する。In the previous paper, it was mentioned that Cu^ and Mn^ inhibited the hydrolysis of pyrophosphate which was the second step of the enzymatic hydrolysis of tripolyphosphate. This work was undertaken to investigate the inhibition mechanism with Cu^ and Mn^ in the enzymatic hydrolysis of pyrophosphate. The results are summarized as follws ; 1. On a definite condition, substrates are precipitated by Cu^ and Mn^. 2. On the condition that substrates do not precitate, Cu^ inhibits the enzymatic action, but Mn^ hardly inhibits the action. 3. These results suggest that the inhibition of the enzymatic hydrolysis of pyrophosphate with Cu^ is due to both the inhibition of the enzymatic action and the precipitation of substrates pyrophosphate, while the inhibition with Mn^ is due to the substrate depletion by precipitation.departmental bulletin pape
