Abstract
Sphingomyelinase (sphirogomyelin phosphodiesterase EC 3.1.4.12) catalyses the degradation of sphingomyelin to ceramide and phosphocholine. At least two forms of the enzyme have been described in mammalian tissues1,2. One forr has a neutral pH optimum (pH 7.4) and requires Mg++ for activity2,3. Based on its almost exclusive localization in brain, enrichment in grey matter2,4, increase in activity in parallel with neuronal maturation5, and particularly high activity levels in certain anatomical regions of brain with special physiological functions4, we have postulated a specific role for this enzyme in the special physiological functions-of neural tissue.
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© 1986 Plenum Press, New York
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Mohan Das, D.V., Cook, H.W., Spence, M.W. (1986). Control of Surface Sphingomyelinase Activity in Cultured Neuroblastoma Cells. In: Freysz, L., Dreyfus, H., Massarelli, R., Gatt, S. (eds) Enzymes of Lipid Metabolism II. NATO ASI Series, vol 116. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5212-9_69
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DOI: https://doi.org/10.1007/978-1-4684-5212-9_69
Publisher Name: Springer, Boston, MA
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