作者: T.G. Brady , W. O'Connell
DOI: 10.1016/0006-3002(62)90035-5
关键词: Ultracentrifuge 、 Adenosine deaminase 、 Fractionation 、 Specific activity 、 Enzyme 、 Cellulose 、 Adenosine 、 Biochemistry 、 Isoelectric point 、 Chromatography 、 Chemistry
摘要: Abstract Adenosine deaminase (adenosine aminohydrolase, EC 3·5·4·4) has been purified over 200-fold from acetone-dried calf mucosa by acid and acetone fractionation followed chromatography on DEAE-SF cellulose. The enzyme was obtained in 35–45% yield had a specific activity of 430 units (μmoles adenosine/min at 37°). It homogeneous the ultracentrifuge but separated into four enzymeically active components starch-gel electrophoresis. an isoelectric point pH 4.85 optimum 7.0.