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Literature DB >> 7060557

Primary structure of the glycans from human lactotransferrin.

G Spik, G Strecker, B Fournet, S Bouquelet, J Montreuil, L Dorland, H van Halbeek, J F Vliegenthart.

Abstract

The polypeptide chain of human lactotransferrin possesses two glycoslyation sites to which glycans are linked through an N-(beta-aspartyl)-N-acetylglucosaminylamine bond and which are structurally heterogenous. After chymotryptic or pronase digestions, glycopeptides with five different glycan structures could be isolated. For three of them, the structure has been determined by the application of methanolysis, methylation analysis, hydrazinolysis/nitrous deamination, enzymatic cleavage and 1H-NMR spectroscopy at 360 MHz: Glycopeptides A and B: NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)[NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-6)]Man(beta 1-4)GlcNAc(beta-1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-)Asn; Glycopeptide C: NeuAc(alpha 2-6)(Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)(Gal(beta 1-4)[Fuc(alpha 1-3)]GlcNAc(beta 1-2)Man(alpha 1-6))Man(beta 1-4)GlcNAc(beta 1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-)Asn. Glycopeptide D: NeuAc(alpha 2-6)Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-3)[Gal(beta 1-4)GlcNAc(beta 1-2)Man(alpha 1-6)]Man(beta 1-4)Glc-NAc(beta 1-4)[Fuc(alpha 1-6)]GlcNAc(beta 1-)Asn. Two other glycopeptides were obtained in very low amount and possess more complex structures.

Entities: Chemical Gene Species

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Year: 1982 PMID： 7060557 DOI： 10.1111/j.1432-1033.1982.tb05803.x

Source DB: PubMed Journal: Eur J Biochem ISSN： 0014-2956

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Cited

42 in total

1. Lactotransferrin receptor of mouse small-intestinal brush border. Binding characteristics of membrane-bound and triton X-100-solubilized forms.

Authors: W L Hu; J Mazurier; G Sawatzki; J Montreuil; G Spik
Journal: Biochem J Date: 1988-01-15 Impact factor: 3.857

2. Inhibition of the specific binding of human lactotransferrin to human peripheral-blood phytohaemagglutinin-stimulated lymphocytes by fluorescein labelling and location of the binding site.

Authors: D Legrand; J Mazurier; P Maes; E Rochard; J Montreuil; G Spik
Journal: Biochem J Date: 1991-06-15 Impact factor: 3.857

3. Pneumococcal neuraminidases A and B both have essential roles during infection of the respiratory tract and sepsis.

Authors: Sonia Manco; Fidelma Hernon; Hasan Yesilkaya; James C Paton; Peter W Andrew; Aras Kadioglu
Journal: Infect Immun Date: 2006-07 Impact factor: 3.441

4. Molecular modeling of a disialylated monofucosylated biantennary glycan of the N-acetyllactosamine type.

Authors: J Mazurier; M Dauchez; G Vergoten; J Montreuil; G Spik
Journal: Glycoconj J Date: 1991-10 Impact factor: 2.916

5. The N-terminal Arg2, Arg3 and Arg4 of human lactoferrin interact with sulphated molecules but not with the receptor present on Jurkat human lymphoblastic T-cells.

Authors: D Legrand; P H van Berkel; V Salmon; H A van Veen; M C Slomianny; J H Nuijens; G Spik
Journal: Biochem J Date: 1997-11-01 Impact factor: 3.857

6. The protein structure of recombinant human lactoferrin produced in the milk of transgenic cows closely matches the structure of human milk-derived lactoferrin.

Authors: Ellen A J Thomassen; Harrie A van Veen; Patrick H C van Berkel; Jan H Nuijens; Jan Pieter Abrahams
Journal: Transgenic Res Date: 2005-08 Impact factor: 2.788

7. Properties of the iron-binding site of the N-terminal lobe of human and bovine lactotransferrins. Importance of the glycan moiety and of the non-covalent interactions between the N- and C-terminal lobes in the stability of the iron-binding site.

Authors: D Legrand; J Mazurier; D Colavizza; J Montreuil; G Spik
Journal: Biochem J Date: 1990-03-01 Impact factor: 3.857