The anticomplementary activity of the rabbit lens.
We wished to determine if inhibitors of the complement system are present in the normal rabbit lens. Soluble less extract in various dilutions was incubated with normal human serum (as source of complement). The residual hemolytic activity was measured using sheep erythrocytes sensitized with antisheep rabbit hemolysin. The lens extract was found to contain two heat stable anticomplementary factors of different molecular weights capable of cleaving C2 and C4. Gel filtration showed that one of these factors was located in the alpha-crystalline region. It is suggested that the anticomplementary factors in the lens may be related to a natural mechanism for the modulation of complement mediated lens injury.
D000328:Adult; D000818:Animals; D000937:Antigen-Antibody Reactions; D001323:Autoantibodies / Q000276:immunology; D002850:Chromatography, Gel; D003175:Complement C2 / Q000037:antagonists & inhibitors*; D003181:Complement C4 / Q000037:antagonists & inhibitors*; D003169:Complement Inactivator Proteins / Q000276:immunology*; D003470:Culture Media; D046508:Culture Techniques; D006358:Hot Temperature; D006801:Humans; D007908:Lens, Crystalline / Q000276:immunology*; D011817:Rabbits
D001323:Autoantibodies; D003175:Complement C2; D003181:Complement C4; D003169:Complement Inactivator Proteins; D003470:Culture Media