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Identification and Characterization of Protein Glycosylation using Specific Endo- and Exoglycosidases
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Galactosylated proteins are recognized by the liver according to the surface density of galactose moieties

M Nishikawa1, C Miyazaki, F Yamashita

  • 1Department of Drug Delivery Research, Faculty of Pharmaceutical Sciences, Kyoto University, Japan.

The American Journal of Physiology
|May 1, 1995
PubMed

The recognition of 111In-labeled galactosylated superoxide dismutase (Gal-SOD) and galactosylated bovine serum albumin (Gal-BSA) by the liver was investigated in mice after intravenous injection. 111In-labeled galactosylated proteins were recovered in the liver by amounts that were highly dependent on the degree of galactose modification and the administered dose. The distribution patterns were analyzed based on a physiological pharmacokinetic model including an uptake process with Michaelis-Menten kinetics in the liver and hepatic plasma flow. The Michaelis constant of hepatic uptake of 111In-Gal-SOD was observed to inversely correlate with the number of galactose residues, without a significant change in maximum rate of uptake or extrahepatic clearance. This relation could be applied to 111In-Gal-BSA and other galactosylated proteins by using the surface density of galactose residues as a degree of modification, suggesting galactose density controls ligand recognition by the asialoglycoprotein receptor. The analysis also indicated that increasing galactose density higher than 1.0 x 10(-3) molecules/A2 did not affect the distribution of galactosylated proteins due to limitation by the hepatic plasma flow rate. In conclusion, efficient delivery of proteins modified with galactose to the liver will be achieved by controlling both the galactose density on the protein surface and the administered dose.

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