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- and
-Interferon
Istituto di Fisiologia Generale Università, 53100 Siena, Italy
1 Istituto Sieroterapico A. Sclavo, Siena, Italy
The susceptibility of human leukocyte (
), fibroblast (
) and recombinant
-2-interferons to clearance by the isolated and perfused rabbit liver has been evaluated. Human leukocyte and recombinant
-2-interferons were stable and their initial levels were maintained in the perfusate even if they had been treated with neuraminidase, thus suggesting that
-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.
Keywords: interferons, asialointerferons, liver catabolism, hepatic binding protein
Received 10 November 1981;
accepted 5 February 1982.
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