Abstract
Soluble supernatant fluids obtained from disrupted human lymphocytes were fractionated by gel filtration and ion exchange chromatography. Three populations of antibody molecules were obtained. One of these was a fragment of γG globulin; the remaining two were γG globulins immunologically indistinguishable from serum γG globulins. Of these last two populations, one was associated with residues of ribonucleic acid; the other with residues of deoxyribonucleic acid. The latter was linked by a disulphide bond to an acidic acceptor protein; the acceptor in turn appeared chemically bound to nuclear DNA. Uptake of antigen by lymphocytes occurred only when antibody was bound to the acceptor (activated antibody).
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Selected References
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