Isolation and characterization of mouse C1q.
C1q was isolated from mouse serum and ascites fluid by absorption onto human IgG-coated latex beads followed by separation on 3-10% exponential gradient sodium dodecyl sulfate (SDS) polyacrylamide gels. Mouse C1q was also purified by low ionic strength precipitation of mouse serum. The purified C1q was heat-labile (56 degrees C, 30 min) both structurally and functionally, contained 4.3% hydroxyproline, 1.38% hydroxylysine, and 18.5% glycine, had an apparent molecular weight of 380,000 daltons, and reconstituted the hemolytic complement activity of C1q-depleted mouse serum. The negatively stained ultrastructural appearance of this purified material consisted of 6 globular units connected by strands. These data demonstrate that mouse C1q structurally and functionally is similar to human and rabbit C1q. A portion of polyacrylamide gel containing mouse C1q was injected into rabbits resulting in the production of monospecific antisera against mouse C1q. Thus, this procedure is a new, rapid and simple method to obtain monospecific antisera against mouse C1q.
D000327:Adsorption; D000596:Amino Acids / Q000276:immunology; D000818:Animals; D000917:Antibody Formation; D001202:Ascitic Fluid / Q000276:immunology; D003172:Complement C1 / Q000276:immunology / Q000302:isolation & purification* / Q000502:physiology; D004591:Electrophoresis, Polyacrylamide Gel; D006461:Hemolysis; D006801:Humans; D007106:Immune Sera / Q000276:immunology; D008722:Methods; D051379:Mice; D011233:Precipitin Tests; D011817:Rabbits
D000596:Amino Acids; D003172:Complement C1; D007106:Immune Sera