The glycopeptides of fetuin and γ G immunoglobulin have been covalently linked to lysozyme and albumin with the coupling reagent toluene 2,4 diisocyanate. When the fetuin glycopeptide-protein compounds were treated with neuraminidase to remove sialic acid, and then injected into rats, the coupled compounds were rapidly and selectively removed from the circulation by the liver, most likely by the hepatocytes. Removal of the exposed galactose residues of the asialofetuin-proteins with β-galactosidase prevented this clearance. Neither the native proteins nor the γ G glycopeptide-proteins are taken up by the liver, demonstrating the specificity of the phenomenon. Once the asialofetuin-protein complexes enter the hepatocytes, they are degraded within two hours.
|Number of pages||8|
|Journal||Biochemical and Biophysical Research Communications|
|State||Published - Nov 5 1971|