Immune complex receptors on cell surface. I. Ultrastructural demonstration of macrophages.
A method is described for ultrastructural localization of immune complex receptors on the surface of viable peritoneal exudate cells. The technique entails incubation with a soluble complex of horseradish peroxidase (HRP) and specific antibody to HRP at 4 degrees C followed by exposure to diaminobenzidine and processing for electron microscopy. The bound immune complexes were evident as focal deposits of HRP reaction product, adhering closely to the external surface of macrophages with an uninterrupted periodicity varying between 30 and 120 nm. Following incubation with an insoluble immune complex containing a higher proportion of antibody, receptor sites stained frequently, but large aggregates adhered to the cells. Rinsing cells after staining with soluble complexes partially displaced the bound immune complexes. Fixation prior to exposure to immune complexes largely eliminated the binding capacity of the immune complex receptors.
D000818:Animals; D000936:Antigen-Antibody Complex / Q000378:metabolism*; D001666:Binding Sites, Antibody; D002462:Cell Membrane / Q000276:immunology / Q000648:ultrastructure*; D006651:Histocytochemistry; D008264:Macrophages / Q000276:immunology / Q000648:ultrastructure*; D008722:Methods; D008854:Microscopy, Electron; D010544:Peroxidases; D010873:Pinocytosis; D011817:Rabbits; D013194:Staining and Labeling
D000936:Antigen-Antibody Complex; D010544:Peroxidases