Chemical Studies on the Porcine Myelin Basic Protein
An encephalitogenic myelin basic protein was isolated from fresh frozen pig brains by acid- acetone extraction and purified to homogeneity by CM-ceilulose column chromatography and gelfiltration on a Sephacryl S-200 column. In addition to its ability to induce experimental encephalomyelitis in guinea pigs, this protein exhibited the characteristic properties of mammalian myelin basic proteins: high content of glycine and basic amino acid residues: presence of methylated arginine residues and absence of cystine or cysteine: absence of a-helix as revealed by circular dichroic studies in aqueous solution and high isoelectric point. The molecular weight as determined by SDS-polyacrylamidegel electrophoresis was around 20,000, in contrast to 36,000 obtained by gel-filtration on a Sepnadex G-100 column. The latter value suggests that the protein might exist as dimers in aqueous solution.
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- Eylar, EH, Kniskern, PJ and Jackson, JJ (1974) Myelin basic proteins., In: Methods in Enzymology ( Fleischer, S and Packer, L, eds.) Vol. 32, pp. 323–341, Academic Press, New YorkGoogle Scholar