CHARACTERIZATION OF THE ANTIGEN (GP600) OF HEYMANN NEPHRITIS

  • 1 January 1984
    • journal article
    • research article
    • Vol. 50  (3) , 287-293
Abstract
The nephritogenic brush border glycoprotein antigen (gp600) of autoimmune membranous glomerulonephropathy (Heymann nephritis) isolated from crude [rat] proximal renal tubular membrane fraction (FX1A) by Lens culinaris lectin affinity chromatography was characterized. The MW of the antigen determined by molecular exclusion chromatography was 600,000 [daltons]. On sodium dodecyl sulfate-polyacrylamide gel electrophoresis is resolved into 5 polypeptides which were in the MW range of 70,000 to 330,000. All 5 polypeptide bands stained for carbohydrates and lipids with Schiff''s reagent and Sudan black, respectively. Rabbits immunized with gp600 produced an antibody that specifically reacted with the brush border of proximal renal tubules of rat by indirect immunofluorescence and gave a single precipitin line in double diffusion in gel (Ouchterlony) against the antigen. The specificity of gp600 was proven by the ability of gp600 to produce active Heymann nephritis, the ability of anti-gp600 to produce passive Heymann nephritis and the ability of gp600 alone, out of other antigens in FX1A, to specifically react with the nephritogenic autoantibody. The latter was tested by an enzyme immunodiffusion technique described in this report.