Rheumatoid arthritis: an immune complex disease? A review of the reaction of antigen with antibody to form immune complexes and the mechanisms by which they mediate tissue injury.
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Biomedical subjects
Publications and source records attributed to J C Bennett.
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The use of 0.2 M NaOH as a solvent for modification of arginine residues by 1,2-cyclohexanedione in disulfide containing proteins is destructive to the disulfide bonds. Modification can be conveniently done in 0.1 M triethylamine (pH 10.9) without any deleterious effect. Lysozyme was found to retain all its enzymic activity in 0.1 M triethylamine (pH 10.9) whereas complete loss of activity took place in 0.2 M NaOH.
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The immune IgM-like macroglobulins were isolated from three species of bony fishes (Ictalurus punctatus, Lepisosteus osseus, and Polyodon spathula) representing the three orders of the subclass Actinopterygii. These macroglobulins were found to have sedimentation coefficients of 14 S and molecular weights of 600,000-630,000. The carbohydrate compositions were determined and found to be different from that of human macroglobulins. After reduction and alkylation, the heavy and light chains could be separated by gel filtration and were found to have molecular weights of approximately 70,000 and 23,000 respectively. The amino acid compositions of these chains were similar to those of mammalian IgM heavy and light chains. The macroglobulins were found by electron microscopy to have a tetrameric structure, in contrast to the pentameric structure found in mammalian, chicken, and shark IgM, i.e. in species later on the evolutionary scale.
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