Separation of phosphatase isoenzymes by gelfiltration

The demonstration of tissue specific isoenzymes of lactic dehydrogenase and their variations in certain diseases (1, 2, 3) has invigorated the interest for further fractionation of other serum enzymes. Recently FLODIN and KILLANDER (4) have reported on the fractionation of human serum proteins by filtration through porous dextran gel "Sephadex G-200" (4). This method exposes the proteins to very mild conditions and the fractionation is independent of variations in pH. The method therefore seemed especially suitable for separation of enzymes. — This report concerns preliminary results of fractionation by gelfiltration of alkaline and acid phosphatases obtained from various sources known to be rich in these enzymes.