Abstract
By reacting rabbit IgG with Protein A of Staphylococcus aureus (SpA) in a wide range of molar ratio only one type of complex was formed with a mol. wt of 350,000 daltons and a molar composition of IgG 2-SpA 1. The IgG 2-SpA 1 complex is not able to bind SpA pointing out that the Fc region binding sites of IgG are saturated by SpA. The inability of IgG 2-SpA 1 complex to bind rabbit IgG as compared with its ability to react with rabbit IgG when fixed to sheep erythrocytes or to Sepharose beads, and to precipitate human IgG suggests that on SpA molecule there are four combining sites with different affinities for IgG. On the basis of these results a hypothetical model of IgG 2-SpA 1 complex is presented.
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