Pharmacokinetics and organ distribution of cationized colchicine-specific IgG and Fab fragments in rat.

Pharmacokinetics of cationized goat colchicine-specific polyclonal immunoglobulin G (IgG) and antigen binding fragment (Fab) (cIgG and cFab, respectively) were studied in male adult Sprague-Dawley rats and compared with those of the native proteins (nIgG and nFab). All proteins were radioiodinated by the Iodogen method, and kinetics were investigated following trichloroacetic acid (TCA) precipitation or immunoprecipitation. Deiodination and catabolism were more pronounced with the cationized than the native proteins, especially for cFab.

Renal tolerance of digoxin-specific Fab fragments in the rat.

Renal markers were investigated over 96 h in male Sprague-Dawley rats after i.v. administration of 10.

Hepatic disposition and toxicity of cationized goat immunoglobulin G and fab fragments in isolated perfused rat liver.

Colchicine-specific goat IgG and Fab fragments were cationized by covalent coupling of hexamethylenediamine. The immunoreactivity of antibodies was not changed following cationization. The interaction of 125I-radiolabeled native (nIgG and nFab) and cationized immunoglobulin G (cIgG) and Fab fragments (cFab) with liver was investigated using isolated perfused rat liver (IPRL) and isolated rat hepatic parenchymal cells (PCs) and nonparenchymal cells (NPCs) in suspension.

Interspecies scaling of clearance and volume of distribution for horse antivenom F(ab')2.

F(ab')2 fragments are sometimes preferred to whole IgG for therapeutic or diagnostic uses. Preclinical pharmaceutical development studies are necessary before their use in humans. Here we propose an allometric approach among three mammalian species to predict F(ab')2 pharmacokinetic parameters in humans.

Pharmacokinetics of heterologous and homologous immunoglobulin G, F(ab')2 and Fab after intravenous administration in the rat.

Because few pharmacokinetic studies of antibodies and their fragments have compared the influence of species origin and antibody size, the plasma pharmacokinetics of a single intravenous dose (0.7 mg kg-1) of 125I-labelled mouse, rat and human immunoglobulin G (IgG), and mouse F(ab')2 and Fab were investigated in the rat. IgG reached equilibrium after six distribution half-lives, i.

Interspecies scaling of clearance and volume of distribution for digoxin-specific Fab.

Digoxin-specific Fab are recognized to be effective in the treatment of acute cardiac glycoside poisoning but no pharmacokinetic studies have been performed in human volunteers. We thus propose an allometric approach among three mammalian species to predict Fab pharmacokinetic parameters in humans. Plasma disposition of digoxin-specific Fab was studied at a 20 mg/kg i.

Immunoglobulin G, F(AB')2, and fab fragment uptake kinetics in isolated perfused rat liver and rat hepatic cells.

The interaction of 125I-radiolabeled immunoglobulin G (IgG), F(ab')2, and Fab fragments with different modes of production (polyclonal or monoclonal), belonging to different subclasses (IgG1 and IgGT) and derived from different sources (mouse, rat, and horse) with liver, was investigated by using isolated perfused rat liver and isolated rat hepatic parenchymal cells (PCs) and non-parenchymal cells (NPCs) in suspension. Lactosaminated-bovine serum albumin (Lac-BSA) and formaldehyde-bovine serum albumin were used as markers of specific binding to PCs and NPCs, respectively. Using the isolated perfused rat liver model, data clearly indicated a very weak hepatic extraction ratio (< 0.