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Abstract— Myelin was purified from the peripheral nervous system (PNS) of several species. The protein composition of these preparations was examined by discontinuous polyacrylamide gel electrophoresis in buffers containing sodium lauryl sulphate. Proteins characteristic of all samples include, in order of increasing mobility: a series of high molecular weight proteins, the major peripheral nerve protein (P 0 ), two uncharacterized proteins, and two basic proteins (P 1 and P 2 ). Quantitative results, obtained by densitometry of gels stained with Fast Green showed differences in protein distribution, both between species, and from different types of nerves obtained from the same animal. The relative amounts of P 1 and P 2 proteins were the most variable; e.g. myelin from guinea‐pig sciatic nerve had little or no P 2 protein, whereas 15 per cent of the myelin protein of beef posterior intradural root was Pz protein. P 0 , P 1 and P 2 proteins from rabbit sciatic nerve and P 0 and P 2 proteins from beef dorsal and ventral intradural roots were purified and their amino acid compositions were determined. Our results indicated that the P 1 protein is very similar in size and amino acid composition to the basic protein of central nervous system myelin, whereas the P 0 and P 2 proteins are unique to the PNS.
Greenfield et al. (Sun,) studied this question.