Abstract
Cerebrospinal fluid was concentrated in cellophane bags, which had a glass container tied into the bottom to predetermine the volume of concentrate, by dialysis against polyvinylpyrrolidone and submitted to electrophoresis for 6 hours in starch gel which was prepared from pre-hydrolised starch with borate buffer in plastic molds. The proteins were stained with naphthalene black B 200 and lipoproteins with oil red 0. 10-12 protein fractions were seen normally in an arrangement similar to the serum protein pattern except for quantitative differences in prealbumins and alpha, beta and gamma fractions. In disease states additional distinct fractions appeared in gamma and prealbumin regions and were designated as fast gamma and 3d and 4th prealbumins; alpha and beta sub-fractions showed changes in definition and quantity. The additional fractions were not seen in the serum of the same patients. Alpha-1 lipoproteins migrated in postalbumin area; beta lipoproteins migrated close to the point of application and were seen inconstantly.