The absence of a role for the carbohydrate moiety in the binding of apolipoprotein B to the low density lipoprotein receptor.
The binding of low density lipoprotein (LDL) to fibroblasts occurs through apolipoprotein B, a glycoprotein. The role of the carbohydrate in binding was assessed in two ways: (1) LDL, freed of sialic acid and most of the glucosamine and hexoses by digestion with a mixture of glycosidases, bound to fibroblasts as does native LDL. (2) The glycopeptides liberated from apoprotein B by trypsin and pronase failed to inhibit LDL binding to fibroblasts. Apparently the carbohydrate moiety of LDL does not interact with the plasma membrane receptor.
D001053:Apolipoproteins / Q000378:metabolism*; D002241:Carbohydrates / Q000494:pharmacology*; D005347:Fibroblasts / Q000378:metabolism; D005944:Glucosamine / Q000494:pharmacology; D006026:Glycoside Hydrolases / Q000494:pharmacology; D006601:Hexoses / Q000494:pharmacology; D008077:Lipoproteins, LDL / Q000378:metabolism*; D011955:Receptors, Drug / Q000378:metabolism*; D012794:Sialic Acids / Q000494:pharmacology
D001053:Apolipoproteins; D002241:Carbohydrates; D006601:Hexoses; D008077:Lipoproteins, LDL; D011955:Receptors, Drug; D012794:Sialic Acids; D006026:Glycoside Hydrolases; D005944:Glucosamine