Arylsulfatases of human lung carcinomas at surgery and transplanted to athymic mice were investigated. The activity levels of the arylsulfatases from these carcinomas of various histological types were markedly elevated as compared to those in normal lung. Increment of the activities was higher in the transplanted carcinoma than in the tumor at surgery, possibly due to a larger population of carcinoma cells in transplanted carcinoma tissue.
When arylsulfatases were fractionated by an anion-exchange chromatography, normal lung revealed a basic arylsulfatase B and an anionic arylsulfatase A, while carcinoma tissue contained another component (B1) in addition to A and B enzymes. The arylsulfatase B1 had the same enzymatic properties as arylsulfatase B of normal lung and carcinoma, but differed in its net charge which displayed an anionic shift from the B enzyme. Since sialidase treatment of B1 enzyme resulted in conversion of B1 enzyme to B enzyme with respect to net charge. it is most probable that B1 enzyme is a modified form of B enzyme due to sialidation during the cancerization process. The extent of sialidation modification was much more prominent in transplanted carcinoma that carcinoma at surgery.