A wide variety of synthetic polypeptide antigens bind to serum proteins. There is no evidence for an in vivo binding mechanism, since the binding patterns are the same whether the antigens are injected into the rabbit or mixed with serum in vitro. The glutamic acid-rich polymers bind to more serum proteins than the lysine-rich polymers and a polymer containing equal amounts of glutamic acid and lysine shows a binding pattern intermediate between those of the glutamic acid-rich and lysine-rich polymers. There is no optical determinant to binding, because both the D- and L-enantiomorphs of a synthetic polypeptide show identical binding patterns under a wide variety of conditions.

The conclusions concerning the binding patterns of synthetic polypeptides to serum proteins are consistent over a wide range of electrophoretic conditions (pH 5.5–10.6) in a given animal species and among several different species (rabbit, dog, guinea pig, and ox).

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