Über die Nierenphosphatase. (1. Mitteilung zur Kenntnis der Phosphatasen.)

Abstract

Liberation of phosphatase in kidney autolysis was more complete when toluene was used, but the product was purer when ethyl acetate was employed. The addition of 25-30% alcohol to the autolysis mixture prevented the solution of impurities. Further purification (up to 5000 times the activity of the original kidney) was effected by fractional precipitation with alcohol. Dialysis led to a slow destruction of the enzyme. Purified kidney phosphatase was most active at pH 9. Its molecular weight, by the diffusion method, was 6000-10000.