The term "affinity electrophoresis" which the interaction, and sometimes precipitation was suggested in analogy to affinity chro-occurs. Some modifications of this method matography (l-3) should, in principle, de-are analogous to rocket immunoelectronote all techniques in which charged mole-phoresis, fused-rocket electrophoresis, classicules (A) move in an electric field within a cal Grabar immunoelectrophoresis, and medium containing molecules B capable of crossed immunoelectrophoresis, as reviewed interaction with A resulting in AB com-by Bog-Hansen (5,7). The chief advantage plex formation. Such a definition would also of the use of lectins, as compared with include some immunoelectrophoretic tech-antibodies, for the identification and quanniques (i.e., those in which antibody is titation of glycoproteins by immunoelectroincorporated in the gel) in which the interacphoresis-like affinity electrophoresis ( 7) is tion between A (antigens) and B (antibodies) that the interaction, is not affected by deleads to insoluble precipitate formation. naturation of the glycoproteins. Of course, Despite this principal similarity between this approach is not limited only to the study immunoelectrophoresis and "true" affinity of lectin-glycoprotein interactions; the bindelectrophoresis, the former techniques will ing of staphylococcal protein A to immunonot be discussed in this article. Short re-globulins (8) and interactions of a glial proviews on affinity electrophoresis have been tein with small group-specific ligands (9) published recently (4-6).
were also studied in this way.