Abstract
Three solid-phase forms of human Ig[immunoglobulin]G were compared for their ability to function as the binding target in an enzyme immunoassay for IgM-class rheumatoid factor (RF). IgG was directly adsorbed to polystyrene beads (method A), or immunologically (method B) or covalently (method C) bound to protein adsorbed to beads. C is the method of choice for the preparation of the RF assay solid-phase IgG.