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Human serum contains a lectin which inhibits hepatic uptake of glycoproteins
Author(s) -
Taylor Maureen E.,
Summerfield John A.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81018-2
Subject(s) - glycoprotein , lectin , mannose , biochemistry , in vitro , receptor , chemistry , affinity chromatography , mannose receptor , membrane glycoproteins , n acetylglucosamine , molecular mass , enzyme , macrophage
Human serum will inhibit the specific uptake of N ‐acetylglucosamine‐terminated glycoproteins by isolated rat hepatic sinusoidal cells. The serum inhibitors are not glycoproteins that bind to the hepatic mannose/ N ‐acetylglucosamine receptor but have the properties of lectins which bind to mannose/ N ‐acetylglucosamine‐terminated glycoproteins. They can be isolated from serum by affinity chromatography. The predominant lectin, with a molecular mass of less than 35 kDa, will inhibit the sinusoidal cell uptake of glycoproteins in vitro.