ゴウシュウマダイ筋肉のAMPデアミナ-ゼの精製

概要

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AMP deaminase (EC 3. 5. 4. 6) which catalyzes the deamination of AMP to IMP was solu-bilized from the skeletal muscle of the snapper Pagrus auratus with potassium phosphate buffer (pH 7.0) containing 0.1M KCl and 1mM 2-mercaptoethanol, and purified by ammonium sul-fate fractionation and three steps of column chromatography on cellulose phosphate P11, 5'AMP Sepharose 4B, and Butyl-Toyopearl 650S. The purified enzyme was shown to be homogeneous by SDS-polyacrylamide gel electrophoresis and the specific activity of the enzyme was 40.7 units/mg protein, showing 254-fold purification. The molecular weight of the native enzyme was estimated to be 3.12×105 by gel filtration and 8.2×104 by SDS-polyacrylamide slab gel electrophoresis. These results suggest that the native enzyme has a tetrameric struc-ture and that it has somewhat larger molecular weight than that of AMP deaminases from the muscle of other species.
日本水産學會の論文