Isolation and immunochemical study of a soluble cerebellar lectin delineating its structure and function.
A procedure of sequential extractions of cerebellar tissue was set up, which allowed specific solubilization of endogenous lectins by mannose. Two cerebellar soluble lectins, CSL1 (Mr = 33,000) and CSL2 (Mr = 31,500), were isolated. They appeared to consist of structurally and immunologically related polypeptides chains. By immunoaffinity, another minor component (Mr = 45,000) was isolated. Immunological studies suggested that the minor component is the precursor of the two other, i.e., CSL1 and CSL2, subunits. CSL1 (mainly lysosomal) possesses an additional peptide compared with CSL2 (mainly cytoplasmic and extracellular), which seems to be implicated in the signal for secretion and release.
D000375:Aging; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002531:Cerebellum / Q000032:analysis*; D011232:Chemical Precipitation; D002845:Chromatography; D004591:Electrophoresis, Polyacrylamide Gel; D000939:Epitopes / Q000276:immunology; D006651:Histocytochemistry; D007118:Immunoassay; D037102:Lectins / Q000276:immunology / Q000302:isolation & purification*; D008358:Mannose; D008970:Molecular Weight; D051381:Rats; D011919:Rats, Inbred Strains; D012995:Solubility
D000596:Amino Acids; D000939:Epitopes; D037102:Lectins; D008358:Mannose