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Horseradish peroxidase (HRPO) conjugated with goat antihuman IgG, goat antihuman IgM, and aggregated human IgG has been used as a enzymatic marker to stain IgG, IgM, and rheumatoid factor in rheumatoid cartilage. When HRPO‐anti IgG and HRPO‐anti IgM were used, immunoglobulin deposits were not observed in nonrheumatoid cartilage. However 7 of 8 rheumatoid cartilage specimens stained with HRPO‐anti IgG showed electron‐dense deposits. Three rheumatoid specimens stained with HRPO‐anti IgM showed similar findings. Both of 2 rheumatoid specimens also stained positively with HRPO conjugated with aggregated IgG, a finding indicating that rheumatoid factor was present. The deposits were seen between the collagen fibers of the superficial layer of the cartilage to a maximal depth of 22 m̈ from the surface (average: 7 m̈). The amorphous fibrinous material on the surface of the cartilage was also stained. The demonstration of IgG, IgM, and rheumatoid factor in the superficial zone of rheumatoid cartilage suggests that immune complexes are deposited in the cartilage in this disease.

Antibody synthesis in anamnestic lymphoid cells, measured by incorporation of leucine-C14 into specific antibody, was inhibited at moderate concentrations of actinomycin D. This was accompanied by marked inhibition of synthesis of RNA as measured by incorporation of H3-cytidine monophosphate. However, at low concentrations of actinomycin D, antibody synthesis was unaffected or even increased while RNA synthesis continued to be inhibited. The results obtained suggest that messenger RNA for antibody synthesis, either because it is relatively stable or present in excess, does not become a limiting factor until its synthesis is maximally inhibited. Puromycin, an inhibitor of amino acid coupling, abolished antibody synthesis in low concentration. 6-Mercaptopurine had no effect on the synthesis of antibody or RNA even at high concentration. The data obtained support the view that antibody synthesis follows pathways similar to those utilized for the formation of other types of proteins.