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peptide L was further cleaved by cyanogen bromide, two peptides, peptide J (residues 1-20) and peptide D (residues 21-115), were obtained. Peptide J was inactive in inducing EAE, while peptide D was as weakly active as peptide L. Conformational studies and identical rate of tryptic hydrolysis Experimental allergic encephalomyelitis is an autoimmune disease induced by the basic protein of CNS* 1 myelin (Laatsch et al., 1962;Einstein et al., 1962; which comprises 30% of the total myelin protein. The protein is believed to have a highly ordered and folded structure and is best described as a prolate ellipsoid with an axial ratio 10:1 (Epand et al., 1974). The ease with which the basic protein can be isolated from myelin suggests that its location in the membrane is that of a so-called peripheral protein. The determination of the amino acid sequence of this protein has facilitated the definition of different encephalitogenic sites in this protein which are: a nonapeptide (residues 113-121

A lipopolysaccharide was isolated from Neisseria meningitidis group B by phenol/water extraction and purified by differential ultracentrifugation. This preparation exhibited endotoxic properties as shown by the limulus-lysate assay. Mild acid hydrolysis of the lipopolysaccharide yielded a lipid A fraction and a polysaccharide fraction. The lipid A fraction contained fatty acids, phosphorus and glucosamine. Analysis of the polysaccharide fraction revealed the presence of glucose, galactose, glucosamine, 2-keto-3-deoxyoctonic acid and phosphorus. There was no heptose.

The specific capsular polysaccharide of type 45 Streptococcus pneumoniae was isolated in pure form by chemical and chromatographic methods and found to be a high-molecular-weight, glycosidically linked polymer of a hexasaccharide repeating unit composed of D-galactose (2 mol), L-rhamnose (1 mol), N-acetyl-Dglucosamine (1 mol), N-acetyl-D-galactosamine (1 mol), N-acetyl-L-fucosamine (1 mol), and phosphate (1 mol).

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