Separation of L-Asparaginase-like Substance from Male Human Urine

Abstract

An attempt was made to detect L-asparaginase activity in adult male human urine and to separate the active principle therefrom. With condensation by salting-out with ammonium sulphate, it was found that original urine contains 0.1-2.1 enzyme units of active principle per 100 litres. Its optimal pH is 8.0 with a stable range of pH 9.0-7.0. The elution pattern as observed, using Sephadex G-100, reveals a mono-peak in enzyme activity, whose molecular weight is about 56000 as against 130000-140000 for E. coli-deriving L-asparaginase. Electrophoretically, its migrative pattern is also different from that of E. coli-deriving L-asparaginase.