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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概要

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• The crude enzyme solution was obtained by homogenizing bonito muscle in water, dialysing with water and centrifuging. The optimum pH of the crude enzyme solution was 5.0 and 9-10, and the activity at pH 6.0 was remarkably increased by the addition of 0.01M Mg2+. 5'-Nucleotidase was separated and purified from bonito muscle by extraction with water, ammonium sulfate fractionation, DEAE-cellulose column chromatography and Sephadex G-200 gel filtration. By ammonium sulfate fractionation (30-70% saturation), 54% of the total activities of 5'-nucleotidase were recovered. On purification by DEAE-cellulose chromatography, high specific activity found in the fraction of 0.005M Tris-acetate buffer containing 0.2MNaCI. Combined fractions were concentrated with 0.7 saturated (NH4)2SO4, purified by re-chromatography on DEAE-cellulose and gel filtration (Sephadex G-200). It was found that the purified 5'-nucleotidase of bonito muscle had increased about 215 fold in specific activity, and was recognized to be homogeneous on disc electrophoretic analysis.

• 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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