L
Lambertus Dorland
Researcher at Utrecht University
Publications - 59
Citations - 3699
Lambertus Dorland is an academic researcher from Utrecht University. The author has contributed to research in topics: Sialic acid & Nuclear magnetic resonance spectroscopy. The author has an hindex of 32, co-authored 59 publications receiving 3615 citations. Previous affiliations of Lambertus Dorland include Centre national de la recherche scientifique & French Institute of Health and Medical Research.
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Book ChapterDOI
High-Resolution, 1H-Nuclear Magnetic Resonance Spectroscopy as a Tool in the Structural Analysis of Carbohydrates Related to Glycoproteins
TL;DR: This chapter presents literature data on the high-resolution, 1H-NMR spectroscopy of carbohydrates derived from glycoconjugates and discusses the results for carbohydrates related to the glycoproteins of N-glycosylic type.
Journal ArticleDOI
Determination of the primary structures of 16 asialo-carbohydrate units derived from human plasma alpha 1-acid glycoprotein by 360-MHZ 1H NMR spectroscopy and permethylation analysis.
Bernard Fournet,Jean Montreuil,Gérard Strecker,Lambertus Dorland,Johan Haverkamp,Vliegenthart Fg,J.P. Binette,Karl Schmid +7 more
TL;DR: In this paper, the primary structures of the carbohydrate units of human plasma al-acid glycoprotein were determined in a very short period of time using NMR spectroscopy.
Journal ArticleDOI
Newcastle disease virus contains a linkage-specific glycoprotein sialidase. Application to the localization of sialic acid residues in N-linked oligosaccharides of alpha 1-acid glycoprotein.
TL;DR: The results indicate that the Newcastle disease virus sialidase can initiate the selective degradation of N-linked oligosaccharide branches containing the NeuAc alpha 2 leads to 3Gal linkage.
Journal ArticleDOI
Primary structure of the carbohydrate chain of soybean agglutinin : A reinvestigation by high resolution 1H NMR spectroscopy
TL;DR: In this paper, it was shown that the asparagine-linked carbohydrate moiety of agglutinin is homogeneous and possesses the following structure: (formula, see text)
Journal ArticleDOI
The structure of the asialo-carbohydrate units of human serotransferrin as proven by 360 MHz proton magnetic resonance spectroscopy.
Lambertus Dorland,Johan Haverkamp,B.L. Schut,Johannes F.G. Vliegenthart,Geneviève Spik,Gérard Strecker,Bernard Fournet,Jean Montreuil +7 more
TL;DR: The investigation by high-resolution ‘H nuclear magnetic resonance spectroscopy of the structure of the asialoglycopeptide (asialo-glycanAsn) isolated from serotransferrin is described, and the signals of the anomeric protons, the mannose-H-2 protons and the N-acetyl methyl groups were analysed.