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Structure determination of the single glycan of rabbit serotransferrin by methylation analysis and 360 MHz /sup 1/H NMR spectroscopy

Journal Article:

Abstract

The glycopeptide fraction of rabbit serotransferrin (STF) has been investigated applying an original method for the determination of glycan primary structure combining monosaccharide determination, permethylation and 360 MHz /sup 1/H NMR. It is concluded that the highly purified rabbit transferrin contains only 1 glycan chain/molecule. A heterogeneity of the glycan moiety in the sialic acid residues was observed on isolation by paper electrophoresis of a disialylglycopeptide G-1 and a monosialylglycopeptide 2. The primary structure of glycopeptide G-1 deduced on the basis of the data of carbohydrate composition, permethylation analysis and 360 MHz /sup 1/H NMR spectroscopy is identical to the primary structure of human serotransferrin glycan and the glycopeptide G-2 was shown by /sup 1/H NMR spectroscopy, to be a mixture of two isomeric monosialylglycopeptides.
Authors:
Leger, D; Tordera, V; Spik, G; [1]  Dorland, L; Haverkamp, J; Vliegenthart, J F.G. [2] 
  1. Lille-1 Univ., 59 - Villeneuve-d'Ascq (France)
  2. Rijksuniversiteit Utrecht (Netherlands)
Publication Date:
Sep 15, 1978
Product Type:
Journal Article
Reference Number:
AIX-10-429263; EDB-79-074411
Resource Relation:
Journal Name: FEBS (Fed. Eur. Biochem. Soc.) Lett.; (Netherlands); Journal Volume: 93:2
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; TRANSFERRIN; STRUCTURAL CHEMICAL ANALYSIS; ACETYL RADICALS; BLOOD SERUM; CHEMICAL SHIFT; CRYSTAL STRUCTURE; ELECTROPHORESIS; GALACTOSE; HYDROGEN 1; LIQUID COLUMN CHROMATOGRAPHY; MANNOSE; NMR SPECTRA; NUCLEAR MAGNETIC RESONANCE; PEPTIDES; PROTONS; RABBITS; SIALIC ACID; ACYL RADICALS; ALDEHYDES; ANIMALS; BARYONS; CARBOHYDRATES; CHROMATOGRAPHY; ELEMENTARY PARTICLES; FERMIONS; GLOBULINS; GLOBULINS-BETA; HADRONS; HEXOSES; HYDROGEN ISOTOPES; ISOTOPES; LIGHT NUCLEI; MAGNETIC RESONANCE; MAMMALS; MONOSACCHARIDES; NUCLEI; NUCLEONS; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; POLYSACCHARIDES; PROTEINS; RADICALS; RESONANCE; SACCHARIDES; SEPARATION PROCESSES; SPECTRA; STABLE ISOTOPES; VERTEBRATES; 400301* - Organic Chemistry- Chemical & Physicochemical Properties- (-1987)
OSTI ID:
6337727
Country of Origin:
Netherlands
Language:
English
Other Identifying Numbers:
Journal ID: CODEN: FEBLA
Submitting Site:
INIS
Size:
Pages: 255-260
Announcement Date:

Journal Article:

Citation Formats

Leger, D, Tordera, V, Spik, G, Dorland, L, Haverkamp, J, and Vliegenthart, J F.G. Structure determination of the single glycan of rabbit serotransferrin by methylation analysis and 360 MHz /sup 1/H NMR spectroscopy. Netherlands: N. p., 1978. Web.
Leger, D, Tordera, V, Spik, G, Dorland, L, Haverkamp, J, & Vliegenthart, J F.G. Structure determination of the single glycan of rabbit serotransferrin by methylation analysis and 360 MHz /sup 1/H NMR spectroscopy. Netherlands.
Leger, D, Tordera, V, Spik, G, Dorland, L, Haverkamp, J, and Vliegenthart, J F.G. 1978. "Structure determination of the single glycan of rabbit serotransferrin by methylation analysis and 360 MHz /sup 1/H NMR spectroscopy." Netherlands.
@misc{etde_6337727,
title = {Structure determination of the single glycan of rabbit serotransferrin by methylation analysis and 360 MHz /sup 1/H NMR spectroscopy}
author = {Leger, D, Tordera, V, Spik, G, Dorland, L, Haverkamp, J, and Vliegenthart, J F.G.}
abstractNote = {The glycopeptide fraction of rabbit serotransferrin (STF) has been investigated applying an original method for the determination of glycan primary structure combining monosaccharide determination, permethylation and 360 MHz /sup 1/H NMR. It is concluded that the highly purified rabbit transferrin contains only 1 glycan chain/molecule. A heterogeneity of the glycan moiety in the sialic acid residues was observed on isolation by paper electrophoresis of a disialylglycopeptide G-1 and a monosialylglycopeptide 2. The primary structure of glycopeptide G-1 deduced on the basis of the data of carbohydrate composition, permethylation analysis and 360 MHz /sup 1/H NMR spectroscopy is identical to the primary structure of human serotransferrin glycan and the glycopeptide G-2 was shown by /sup 1/H NMR spectroscopy, to be a mixture of two isomeric monosialylglycopeptides.}
journal = {FEBS (Fed. Eur. Biochem. Soc.) Lett.; (Netherlands)}
volume = {93:2}
journal type = {AC}
place = {Netherlands}
year = {1978}
month = {Sep}
}