Experimental inhibition of myelination in spinal cord tissue cultures: Enzyme assays

Seven specific enzyme activities were assayed in embryonic mouse spinal cord cultures during normal development and under conditions of myelination inhibition and disinhibition. Sulfatase A activity in the inhibited and disinhibited cultures was slightly lower than in the normal control cultures. No specific differences for glucose-6-phosphate dehydrogenase, β-galactosidase, β-glucuronidase, acid prosphatase, and NADP-isocitrate dehydrogenase activities were found among these three experimental conditions. However 2′,3′-cyclic nucleotide phosphohydrolase, an enzyme which has been specifically associated with myelin, showed identical patterns of inhibition and disinhibition as were previously observed for sulfatide synthesis.