Evidence for the presence of lectins with mannose specificity in the rat cerebellum.
Two different methods were set up to detect the possible presence of lectin-like molecules with a specificity for mannose-rich glycans in the rat cerebellum. The first, affinity histochemistry, involved the isolation of a particular class of glycoproteins from the cerebella of 11-day-old rats followed by the formation of covalent complexes with horseradish peroxidase and then incubation with cerebellar slices. The second used in vitro interactions between [3H]leucine-labeled proteins, kept in solution, with insolubilized [14C]glucosamine-labeled glycoproteins. The results of both methods are compatible with the presence of lectin-like activities inhibited by high mannose concentrations, but not other sugars. However, the binding sites preferred by these molecules seem to be more than a single mannose residue.
D000818:Animals; D002250:Carbon Radioisotopes; D002531:Cerebellum / Q000032:analysis* / Q000378:metabolism; D002846:Chromatography, Affinity; D003208:Concanavalin A; D005944:Glucosamine / Q000378:metabolism; D006651:Histocytochemistry; D037102:Lectins / Q000302:isolation & purification*; D008358:Mannose; D051381:Rats
D002250:Carbon Radioisotopes; D037102:Lectins; D003208:Concanavalin A; D005944:Glucosamine; D008358:Mannose