Abstract
The carbohydrate-binding specificities of pea lectin and lentil lectin have been determined by testing the ability of radioactively labeled glycopeptides to bind to columns of pea lectin-Sepharose and lentil lectin-Sepharose. The presence of a fucose residue attached to the asparagine-linked N-acetylglucosamine residue of the test glycopeptide was essential for high affinity binding to both pea and lentil lectin-Sepharose but not to concanavalin A-Sepharose. In addition to fucose, 2 alpha-mannosyl residues were required for glycopeptide binding to the pea and lentil lectin-Sepharose columns. Substitution of the alpha-mannosyl residues at C-2 did not prevent their interaction. Substitution of 1 alpha-mannosyl residue at both C-2 and C-4 did prevent glycopeptide binding, but substitution of 1 alpha-mannosyl residue at C-2 and C-6 did not impair binding. Glycopeptide binding to lentil lectin-Sepharose was enhanced by the exposure of terminal N-acetylglucosamine residues on the glycopeptide, whereas binding to pea lectin-Sepharose was enhanced by the exposure of terminal mannose residues. The differences in carbohydrate binding specificity of pea lectin-Sepharose and Con A-Sepharose were exploited to fractionate a mixture of [2-3H]mannose-labeled glycopeptides derived from mouse lymphoma cell glycoproteins.
Highlights
The carbohydrate-bindingspecificities of pea lectin in more detail using glycopeptideswith oligosaccharide chains and lentil lectin have been determined by testing the of varying structure toprobe the sugar requirements for tight ability of radioactively labeled glycopeptidetso bind to binding
These findings demonstrated that both pea and lentil lectin-Sepharose require fucose in the glycopeptide for high affinity binding, whereas Con A-Sepharose does not
The present study confirms that fucose residues in the core region of the immunoglobulin test glycopeptides are the sine qua non for binding to both pea and lentil lectin-Sepharose
Summary
The carbohydrate-bindingspecificities of pea lectin in more detail using glycopeptideswith oligosaccharide chains and lentil lectin have been determined by testing the of varying structure toprobe the sugar requirements for tight ability of radioactively labeled glycopeptidetso bind to binding. In none of these studies test glycopeptide was essential for high affinity bindinghad fucose been recognizedas a determinant, many to both pea and lentil lectin-Sepharose but not to con- of the test glycopeptides did contain fucose residues in the tncttauhoaottenstbiiyhaoro1evntriahponelfeitCsneati-hdr2aaAeuncaae-tdnSs-imdoewlnpeaCe.hnnr-at4Senirluodrobselisedyqsectlu.Ipitrntiierrunseaet-ivdiSddoeedufnnpoiettrhsiooga1afgnlrtlayyoC-ctcsmo-oeo2fppaudcenecopipdnoltutsoiidemsdn,eyeo2nltbsabri.-inpemnSsdrdiueaidinvnbnueg-sgen,tit-couvinofnagrrpdeiseeoparruteeoslcgeoriicafkotidincnitioot-oyaSfrcoeettfpehivhpxeeaeairlramyooaislnalneibegdaeotnllhsedeaendclthegcilnihlgyltaeihcrlcoiladtepifencefsitpcnibnthiity-adySietneecsspsat.othriAbanborgiconhctsdyohedrt.edorWaianctbeeogf-llfibyuioti,muynwndondef-s but substitutionof 1 a-mannosyl residue atC-2 and C- that fucose residues are an important determinant in 6 did not impair binding. The differences in carbohydrate binding specificity of pea lectin-Sepharose and Con A-Sepharose were exploited to fractionate a mixture of [2-3€rJmannose-labeled glycopeptides derived from mouse lymphoma. Sepharose was prepared as described by Adair and Kornfeld [10].Pea lectin-Sepharose, obtained from Dr I. Purified diplococcal j3-galactosidase was a gift from Dr Jacques Baenziger
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