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.