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040 _cCICY
090 _aB-7213
245 1 0 _aSpecificity of Amaranthus leucocarpus syn. hypocondriacus lectin for O-glycopeptides
490 0 _vBiochimica et Biophysica Acta, 1674(3), p.282-290, 2004
520 3 _athis work, we determined a value of 1.0-10-2 M for the association constant of ALL for GalNAc, calculated using fluorescence spectroscopy assays. Using neoglycopeptides obtained by in vitro O-glycosylation, we determined the main features of O-glycopeptides recognized by ALL using molecular dynamics simulations, capillary electrophoresis, and ELISA. Neo-glycopeptides were obtained by in vitro O-glycosylation reaction using microsomal preparations of murine thymocytes, human gastric fundus and colonic mucosa. ELISA assays were performed with peroxidase-labeled murine monoclonal IgG2, n light chain (5D4)antibodies against ALL. Among the in vitro neoglycopeptides, only those of TTSAPTTS containing GalNAc at Thr in #2 and #6 reacted with ALL. Neither the TTSAPTTS glycopeptide, containing a unique GalNAc residue at Thr in #2, nor others (with more than two GalNAc residues)interacted with the lectin. Computational docking assays of the lower energy conformers for interactions between glycopeptides and lectins confirmed that ALL recognized GalNAc residues when they are spaced out in glycan structures, whereas GalNAc residues arranged in clusters prevented interaction with the lectin, indicating that ALL is specific for a special GalNAc-containing motif found in different O-glycoproteins.
650 1 4 _aAMARANTHUS LEUCOCARPUS
650 1 4 _aPLANT LECTIN
650 1 4 _aT- AND TN-SPECIFIC LECTIN
650 1 4 _aO-GLYCAN
700 1 2 _aHernández, P.
700 1 2 _aTetaert, D.
700 1 2 _aVergoten, G.
700 1 2 _aDebray, H.
700 1 2 _aJimenez, M.C.
700 1 2 _aAlvarez, G.
700 1 2 _aAgundis, C.
700 1 2 _aAgundis, C.
700 1 2 _aZenteno, E.
856 4 0 _uhttps://drive.google.com/file/d/1yIkayHCeGjdY6_77mjwhinrcI0TXiMEK/view?usp=drivesdk
_zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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