2004
DOI: 10.4067/s0717-95022004000400008
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RECOGNITION OF N-ACETYLGLUCOSAMINE (GLyNAc) AND POLY-N-ACETYLLACTOSAMINE RESIDUES IN VESSELS OF THE RAT PINEAL GLAND

Abstract: Lectins are proteins with binding sites that recognize a specific sequence of sugar moieties in complex glycoconjugates. In the present study the tomato lectin-Lycopersicon esculentum (LEL) (a selective microglial and endothelial marker) has been reported to recognize specific residues of N-acetylglucosamine (GlyNAc) and poly-N-acetyllactosamine. In the pineal gland the biotinylated LEL was used to investigate the appearance of these sugar residues in the structures of the rats during their development and adu… Show more

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Cited by 2 publications
(4 citation statements)
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“…We also detected a much smallersized band of RDE (II)-treated IgE, around 150 kDa (Fig. 2A, lanes [13][14][15][16]. Moreover, we obtained the same results by CBB staining (Fig.…”
Section: Rde (Ii) Changes the Structure Of Ige But Not Igg Followed By The Reduction Of The Binding Activity To Anti-⑀ Chainsupporting
confidence: 78%
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“…We also detected a much smallersized band of RDE (II)-treated IgE, around 150 kDa (Fig. 2A, lanes [13][14][15][16]. Moreover, we obtained the same results by CBB staining (Fig.…”
Section: Rde (Ii) Changes the Structure Of Ige But Not Igg Followed By The Reduction Of The Binding Activity To Anti-⑀ Chainsupporting
confidence: 78%
“…S4, lanes 3-9), similar to the situation with IgG (Fig. S4, lanes [12][13][14][15][16][17][18]. These results suggest that sialidase is not primarily responsible for the modification of IgE by RDE (II).…”
Section: Characteristic Features Of Glycan Alteration On Rde (Ii)-treated Igesupporting
confidence: 64%
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