Abstract
The susceptibility of human leukocyte (α), fibroblast () and recombinant α-2-interferons to clearance by the isolated and perfused rabbit liver has been evaluated. Human leukocyte and recombinant α-2-interferons were stable and their initial levels were maintained in the perfusate even if they had been treated with neuraminidase, thus suggesting that α-interferons have no exposed sugars recognizable by hepatic binding proteins. On the other hand, native, and particularly desialylated human -interferon, underwent marked hepatic uptake confirming the importance of the liver as a catabolic site for glycosylated interferons.