No abstract

No abstract

No abstract

Guinea pig serum L-asparaginase has been purified ca. 900-fold by a combination of sodium sulfate fractionation, gel filtration with G-200 Sephadex, DEAE-cellulose chromatography, and chromatography on calcium hydroxylapatite. The enzyme appears to be homogeneous as judged by several criteria, including sedimentation equilibrium ultracentrifugation and the appearance of a single arc upon immunoelectrophoresis. A JLm. sevenfold purification of guinea pig serum1 asparaginase was reported some time ago (Meister, 1955). Interest in this enzyme has increased recently, however, both because of its use in assaying for l-

No abstract