Interaction of lectins with proteins of the endoplasmic reticulum and Golgi system of rat liver.
The interaction of glycoproteins of rough and smooth microsomal and Golgi membranes with Sepharose-bound lectins has been studied. One of these lectins was a crude preparation from wheat germ lipase which was found to bind primarily to N-acetyl neuraminic acid. Rough microsomes, smooth microsomes and Golgi membranes contain glycoproteins which bind to Concanavalin A (Con A specific for mannose residues) in decreasing amounts in the order indicated (rough, smooth and Golgi) and to wheat germ agglutinin (WGA, glucosamine-specific) and to the crude lipase preparation in increasing amounts in the order indicated. The small amount of binding of rough microsomes and Golgi membranes to Crotalaria (galactose-specific) increases substantially after neuraminidase treatment. Three submicrosomal particle preparations enriched either in AMPase or in NADH- or NADPH-oxidizing electron-transport enzymes contain glycoproteins which bind Con A and wheat germ agglutinin. The latter binding is sensitive to neuraminidase treatment. Two other submicrosomal particle preparations, both enriched in glucose-6-phosphatase activity, bind preferentially to WGA. This binding is, however, not sensitive to neuraminidase. Prolonged incubation with Ervilia lectin (mannose-specific) inhibits NADH-ferricyanide reductase activity, while the electron-transport chain involving cytochrome b5 is also inhibited by Crotalaria, indicating that both the flavoprotein and the cytochrome b5 are glycoproteins whose oligosaccharide chains have terminal mannose or galactose residues.
D000818:Animals; D004721:Endoplasmic Reticulum / Q000032:analysis*; D006023:Glycoproteins / Q000032:analysis; D006056:Golgi Apparatus / Q000032:analysis*; D007425:Intracellular Membranes / Q000032:analysis; D037102:Lectins / Q000494:pharmacology*; D008099:Liver / Q000648:ultrastructure*; D008297:Male; D008565:Membrane Proteins / Q000032:analysis*; D008862:Microsomes, Liver / Q000032:analysis; D010088:Oxidoreductases / Q000378:metabolism; D051381:Rats; D014357:Trypsin / Q000494:pharmacology
D006023:Glycoproteins; D037102:Lectins; D008565:Membrane Proteins; D010088:Oxidoreductases; D014357:Trypsin