抄録
Cytosine deaminase from Pseudomonas aureofaciens was purified about 480-fold by means of ammonium sulfate fractionation, ethyl alcohol fractionation, chromatography on columns of DEAE-Sephadex A-50 and hydroxylapatite and by gel filtration on a Sephadex G-200 column. The enzyme was homogeneous by the criteria of sedimentation and electrophoretic analysis. The molecular weight of the purified enzyme was estimated to be 630, 000 by gel filtration and consisted of twelve to sixteen identical subunits having a molecular weight of about 45, 000. The enzyme catalyzed the deamination of cytosine and 5-methylcytosine.
