The isolation and properties of experimental allergic encephalitogenic protein.

1. Experimental allergic encephalitogenic (EAE) protein was isolated from ox spinal cord by a modification of the method of Martenson & LeBaron (1966). 2. The protein was examined by acrylamide-gel electrophoresis and its amino acid composition determined. 3. Sedimentation-velocity runs in the ultracentrifuge indicate a molecular weight of about 15100 at pH7.8, and calculation suggests that approx. 137 amino acid residues are present per molecule. 4. Gel-filtration and diffusion studies suggest that the protein is non-globular. 5. Optical-rotatory-dispersion measurements show the protein to have no helical secondary structure even at pH values near to the isoelectric point. In the presence of triphosphoinositide, changes in the optical rotatory dispersion of the protein could be interpreted to mean that it develops a small degree of secondary structure. 6. On treatment with cyanogen bromide the experimental allergic encephalitogenic protein is split into at least two fragments, the larger of which is only about 12% smaller than the parent protein and is antigenically active, and the smaller of which is devoid of antigenic activity.