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Tc-99m Galactosyl-Neoglycoalbumin: In Vitro Characterization of Receptor-Mediated Binding

University of California, Davis
Medical Center, Sacramento, California

Correspondence: For reprints contact: Robert c. Stadalnik, MD, Division of Nuclear Medicine, University of California, Davis, Medical Center, 2315 Stockton Blvd., Sacramento, CA 95817.

ABSTRACT

Heptaic binding protein (HBP) is a membrane receptor that binds and transports plasma glycoproteins from hepatic blood to hepatcocellular lysosomes. We have characterized the in vitro binding of Tc-99m galactosyl-neoglycoalbumin (TcNGA), a synthetic HBP ligand, to liver membrane. Structural modifications of NGA resulted in the alteration of the equilibrium constant, K_A, and the forward-binding rate constant, k_b. Binding was second-order; the relative amount of membrane-bound NGA depended on the initial concentrations of ligand and membrane. Membrane displacement studies, using carrier ligands in contrast to previously bound Tc-NGA or I-NGA, correlated with the binding characteristics of a native HBP ligand, asialo-orosomucoid. We used computer simulation to study the detectability of the changes in HBP concentration at different values of k_b. The simulations indicated that radiopharmacokinetic sensitivity to alterations in [HBP] should be possible using a neoglycoalbumin preparation with a carbohydrate density within the range of 15 to 25 galactose units per albumin molecule.

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