Characterization of seminoma-derived placental-like alkaline phosphatase

Characteristics of placental-like alkaline phosphatase (PLAP-like enzyme) in seminoma was studied. By use of lectin affinity chromatography, PLAP-like enzyme in seminoma revealed extra sugar chains compared to placental alkaline phosphatase (PLAP), indicating heterogeneity of the carbohydrate moiety. However, the glycosylation patterns were found to be essentially similar between seminoma and normal testis. On isoelectric focusing, differences in migration patterns were revealed between seminoma-derived and normal testis-derived PLAP-like enzyme as well as between PLAP-like enzyme and PLAP. The differences in charge were mainly due to differences in sialylation of the molecules. The complex pattern of PLAP-like enzyme from seminoma on isoelectric focusing was not altered by neuraminidase treatment, indicating a considerable charge heterogeneity within the population of the enzyme molecules from the tumor.