PHOSPHOGLYCERATE MUTASE, 2,3-BISPHOSPHOGLYCERATE PHOSPHATASE AND CREATINE-KINASE ACTIVITY AND ISOENZYMES IN HUMAN BRAIN-TUMORS

The distribution of phosphoglycerate mutase (EC 5.4.2.1, PGM), 2,3-bis phosphoglycerate phosphatase (EC 3.1.3.13, BPGP) and creatine kinase ( EC 2.7.3.2, CK) activity and isoenzymes in various regions of adult hu man brain and in brain tumours (astrocytomas, anaplastic astrocytomas, glioblastomas and meningiomas) has been determined using electrophore sis. PGM and cytosolic CK exist in mammalian tissues as three isoenzym es that result from the homodimeric and heterodimeric combinations of two subunits [types M (muscle) and B (brain)] coded by separated genes . In addition, a dimeric from and an octameric form of mitochondrial G K exist in mammals. Type BB-PGM was the major PGM isoenzyme found in n ormal brain, although type MB-PGM and type MM-PGM were also detected. All brain tumours possessed lower PGM activity than normal brain, and meningiomas showed higher BPGP activity. In astrocytic tumours, the pr oportion of type MB-and type MM-PGM decreased, and in meningiomas thes e isoenzymes were not detected. Type BB-CK and mitochondrial CK were t he only CK isoenzymes detected in normal brain. Astrocytomas possessed lower CK activity than anaplastic astrocytomas and glioblastomas and, in addition, tended to possess lower CK content than normal brain. No qualitative changes of the normal CK isoenzyme pattern were observed in the tumours.