Abstract
A naturally occurring antiglobulin factor against the Fab-fragment of homologous IgG, contained in the rabbit and human blood serum and γ-globulin preparations, was shown by gelfiltration on Sephadex G-200 to have a molecular weight of about 250,000 daltons. In man this factor does not pass through the placenta in normal pregnancy. Despite differences in the physicochemical and effector properties of 7S IgG and protein with homoreactant activity, the latter has the specific antigenic determinants of IgG. These observations suggest that a complex of IgG with another protein or nonprotein compound possesses homoreactant properties.
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