KMID : 0378019890320100031
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New Medical Journal 1989 Volume.32 No. 10 p.31 ~ p.37
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Purification and characyerigation of Adenosine Deaminase from Rat Liver
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Abstract
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Adenosine deaminase from rat liver has been purified to electrophoretic homogeneity by ammonium sulfate precipitation, DEAE-Sephadex A-50 chromatography, gel filtration through Sephadex G-100 and affinity column bed material employing adenosine as the ligand. The enzyme was specific toward adenosine and had no activity toward adenine, 5"-AMP, A TP,
guanosine and guanine. The Michaellis constant based on the Lineweaver-Burk plot was 4.5 x 1VM and the optimum pH was about 7.0. The enzyme activity was completely inhbited vy 1 mM Hg2+ and found to be about 86% of original activity in 1 mM Mg2+.
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