Purification by Starch Block Electrophoresis of Renal Antigen that Induces Nephrotoxic Antibody

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Abstract
Summary: Further purification of the antigenic substance in the supernatant substance of trypsin-digested rat kidney cortex homogenate (TR-KH) was achieved using starch block electrophoresis. Almost all the antigenic activity responsible for the production of nephrotoxic antibody was found in fraction -3, which was free of nucleic acid. Rats receiving a single injection of antiserum against fraction -3 showed distinct clinical and histologic changes of typical proliferative glomerulonephritis. Moreover, severe chronic glomerulonephritis (so-called contracted kidney) was induced in rats killed 7 to 9 weeks after a single injection. Studies using the fluorescent antibody technique showed that this purified antigen (fraction -3) is derived from the glomerular basement membrane. This fraction was more highly purified as a single peak by gel-filtration using Sephadex G 200. Fraction -3 is probably a polysaccharide-protein complex, and the results of chemical analysis suggest strongly that the active principle of this antigenic substance is closely related to the polysaccharide moiety.