精製酵素の二,三の性質 (カツオ筋肉の5'-ヌクレオチダーゼに関する研究-1,2-)

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概要

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• Previously, the author reported the purification of 5'-nucleotidase from bonito muscle by extraction with water, ammonium sulfate fractionation, DEAE-cellulose column chromatography and Sephadex G-200 gel filtration. In this paper, studies on some of the properties of the purified 5'-nucleotidase are reported. This enzyme had a pH optimum of 5.5 in the presence of 0.01M Mg2+, with 5'-IMP as substrate. The rate of Pi liberation from 5'-IMP was Tinier for 80 minutes, the rate of hydrolysis decreasing slightly thereafter. This enzyme showed highest relative activity with 5'-IMP as substrate, and also hydro-lyzed other 5'-nucleotides. On the other hand, it did not act on 3'(2')-nucleotides. Of several metal ions Mg2+ was most effective and Fe2+ also activated this enzyme. Ca2+, Mn2+, Fe3+ and Zn2+ inhibited the 5'-nucleotidase activity to 56Y., 70%, 67% and 35 % of the control activity respectively, while Ba2+ completely inhibited this enzyme. The apparent Km value of 1.08 mM and pKm of 2.97 were calculated for 5'-IMP. Using Sephadex G-200 gel filtration, the molecular weight of this enzyme was estimated to be 115, 000.

• 日本水産學會の論文

著者

• 広田 望

  宮城県水産加工研究所

関連論文

• 精製酵素の二,三の性質 (カツオ筋肉の5'-ヌクレオチダーゼに関する研究-1,2-)
• 5'-ヌクレオチダーゼの分離・精製 (カツオ筋肉の5'-ヌクレオチダーゼに関する研究-1,2-)

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