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J. Gagnon, P. R. Finch, DD Wood, and MA Moscarellof abstract: Myelin was extracted first with mercaptoethanol followed by 0.2 n H2S04. The resulting residue was dissolved in chloroform-methanol (1: 1, v/v) containing 5% of 0.1 n HC1 and applied to a Sephadex LH-20 column. The major protein fraction was rechromatographed on a similar LH-20 column. The protein was isolated by precipitating with ether and the precipitate was washed with 2-propanol. It migrated as a single componentin polyacrylamide gel electrophoresis and appeared to be homogeneous by analytical ultracentrifugation. Amino acid analysis revealed it was relatively high in neutral and low in basic residues. A single N-terminal glycine was found. Of the carbohydrates tested, sialic acid,