Two-dimensional immunoelectrophoresis of unconcentrated cerebrospinal fluid.

The two-dimensional immunoelectrophoresis on cellulose acetate, already utilized for serum proteins, has been applied to CSF proteins. The technical modifications which allow the use of unconcentrated CSF are described. By utilizing a particularly suitable supporting medium, a good separation of proteins is achieved; consequently narrow-based peaks are obtained and the isoantigens can be displayed as distinct components in spite of closely similar migration velocities. The preliminary results of this method are given. Particulary interesting appears a beta-migrating protein and the gamma-migrating oligoclonal bands. The first may present an anodic cleavage suggesting that it may be the beta1C/beta1A-globulin. If this hypothesis is confirmed, the relative concentrations of the two components can be investigated. No clear-cut peaks corresponding to the gamma-migrating oligoclonal bands have been observed, their place being taken by a low precipitation line continuous with the IgG peak. The reasons for this phenomenon may be tentatively ascribed to a local specificity of these IgG.