Abstract
2′,3′-Cyclic nucleotide 3′-phosphodiesterase (CNPase, EC 3.1.4.37*) has been widely used for several years as a marker for the presence of myelin in the central nervous system, but no review is available on its application and limitation as a marker enzyme and there is no information on its role in myelin. This was the first enzyme to be unequivocally characterized as a myelin component; previously it had been thought that myelin was enzymatically inert (Adams et al., 1963). Several other enzymes have now been proposed as being myelin-associated (for references see Carnegie and Sims, 1977; Norton, 1977), but evidence of myelin association is incomplete for some of these, such as protein kinase (Carnegie et al., 1974; Miyamoto and Kakiuchi, 1974; Steck and Appel, 1974; Miyamoto, 1976) and phosphoprotein phosphatase (Miyamoto and Kakiuchi, 1975). In the case of nonspecific esterase (Keoppen et al., 1969; Frey et al., 1971; Rumsby et al., 1973; Mitzen et al., 1974) and arylamidase (Banik and Davison, 1969; Riekkinen and Clausen, 1970; Riekkinen and Rumsby, 1972; Mezei and Palmer, 1974) there is some controversy as to whether the enzymes are truly myelin-associated or are bound as an artifact of the preparation of myelin. There is strong evidence that cholesterol ester hydrolase is a myelin enzyme (Eto and Suzuki, 1973). The evidence that CNPase is a true myelin component is presented herein.
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Sims, N.R., Carnegie, P.R. (1978). 2′,3′-Cyclic Nucleotide 3′-Phosphodiesterase. In: Agranoff, B.W., Aprison, M.H. (eds) Advances in Neurochemistry. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-8240-3_1
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