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A biochemical comparison of Xenopus laevis and mammalian myelin from the central and peripheral nervous systems

1978; Wiley; Volume: 9; Issue: 3 Linguagem: Inglês

10.1002/neu.480090304

1097-4695

Richard H. Quarles, N Sakuragawa, J. L. Everly, Carol F. Pasnak, H. deF. Webster, Bruce D. Trapp,

Growth Hormone and Insulin-like Growth Factors

Abstract Myelin purified from the central nervous system of Xenopus laevis contained the same major lipid and protein components as human myelin. However, some minor differences in the myelin proteins were noted. The Xenopus basic protein had a higher apparent mol wt. on sodium dodecyl sulfate gels than the corresponding mammalian protein. The absolute specific activity of 2′,3′‐cyclic nucleotide 3′‐phosphohydrolase in the Xenopus myelin was considerably higher than in mammals. There were differences in the high mol wt. proteins, and the glycoproteins in Xenopus myelin were more heterogeneous than those in mammals. Peripheral myelin from Xenopus sciatic nerve was compared with that from the rat. The lipids in the two types of myelin were similar. There was a major glycoprotein in the Xenopus myelin corresponding to the P 0 protein and a basic protein of slightly larger mol wt. than the P 1 protein of rat myelin.