Isoelectric points and charge-dependent separation of erythrocyte phosphoglucomutase isoenzymes (PGM1 and PGM2).

Phosphoglucomutase can bind both negative and positive ions so that it may change its net electric charge according to the buffer species of the medium. For this reason the knowledge of the pIs of the erythrocyte phosphoglucomutase isoenzymes is not sufficient to forecast their separability by procedures based on charge separations such as ion exchange chromatography. In this paper we indicate the condition to obtain a satisfactory separation of the main erythrocyte phosphoglucomutase isoenzymes by DEAE-cellulose column chromatography. The pI values of the isolated isoenzymes are also reported and compared to those measured by others on whole hemolysates.