Carbohydrate and glycoprotein specificity of two endogenous cerebellar lectins.

摘要: Two endogenous cerebellar mannose binding lectins have been isolated in an active form by immunoaffinity chromatography employing their respective immobilized antibodies. One of them, termed soluble lectin (CSL), was extracted the absence detergents, whereas other, called Receptor 1 (R1), only presence detergents. Tests inhibition agglutination erythrocytes were performed with mono-, oligo and polysaccharides, as well glycoconjugates known structures. On basis agglutinating activities these 2 are different from previously reported brain, since they not inhibited galactosides lactosides marginally glycosaminoglycans. CSL R1 better mannose-rich glycopeptides compared to corresponding oligosaccharides. The patterns obtained glycans structures indicated that very discriminative. Although similar specificities, differed properties towards ovalbumin. Both showed considerable affinity for glycopeptides, also rich mannose. These belong a few Con A-binding glycoprotein subunits present on other glycoproteins. In forebrain, where present, at least some glycoproteins interacting observed cerebellum. Our data overall suggest specific cell recognition nervous system could be invoked via interactions between widely distributed cell-specific