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Binding characteristics of indocyanine green (ICG) to human serum were investigated, with a combination of immunoelectrophoresis and an ICG fundus video system. Serum samples were obtained from three healthy volunteers, 1 minute after intravenous administration of 50 mg/2 ml ICG, and then fractionated immunoelectrophoretically on agarose plates. Electrophoretic patterns on these plates could be observed with an ICG fundus video system as well as an immunoviewer. Using anti-human sera, only one infrared fluorescent line showing the ICG binding immunoprecipitate was recognized near the area of beta fraction, which was also identified by the use of anti-beta-lipoprotein (Lp) antibody. We also studied the affinity of ICG for apolipoproteins (Apo) AI, B, and CIII, which were the main protein components of serum Lps. Electrophoresis showed that ICG bound only to Apo-B, but not to the others. These results indicated that ICG mainly bound to beta-Lp in the blood, and that ICG angiographic patterns were directly reflecting the dynamics of serum Lps, especially for LDL. The high affinity of ICG for only Apo-B could explain the reason why ICG mainly bound to beta-Lp among several serum Lps, because large amounts of Apo-B are included in beta-Lp but a little in other serum Lps.
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