Abstract
Alkaline phosphatase from human liver was extracted by a modified Morton's butanol method and was purified by ammonium sulfate precipitation followed by diethylaminoethyl-cellulose, carboxymethyl-cellulose and Sephadex G-200 column chromatography. Liver alkaline phosphatase thus purified to about 8900-fold with recovery of 10% was demonstrated to be homogeneous by polyacrylamide gel disc electrophoresis.
