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Primary structure of glycans isolated from human leucocyte lactotransferrin. Absence of fucose residues questions the proposed mechanism of hyposideraemia.
- Source :
-
The Biochemical journal [Biochem J] 1990 Aug 01; Vol. 269 (3), pp. 821-5. - Publication Year :
- 1990
-
Abstract
- Lactotransferrin was highly purified from lysates of human neutrophilic leucocytes by immuno-affinity chromatography. A comparative analysis of the molar carbohydrate compositions of human leucocyte lactotransferrin and human milk lactotransferrin reveals that the glycans of leucocyte lactotransferrin differ essentially by the absence of fucose residues. Structural analysis combining methylation-mass spectrometry and 400 MHz 1H-n.m.r. spectrometry of oligosaccharide alditols released from human leucocyte lactotransferrin shows the presence of two disialylated and non-fucosylated biantennary glycans of the N-acetyl-lactosaminic type. These results question a previously proposed mechanism for hyposideraemia in which the leucocyte lactotransferrin was involved and in which the fucose residues played a key role.
- Subjects :
- Anemia, Hypochromic blood
Carbohydrate Sequence
Fucose metabolism
Humans
Hydrazines metabolism
Lactoferrin isolation & purification
Lactoferrin metabolism
Magnetic Resonance Spectroscopy
Mass Spectrometry methods
Milk, Human analysis
Molecular Sequence Data
Oligosaccharides metabolism
Polysaccharides isolation & purification
Lactoferrin blood
Lactoglobulins blood
Leukocytes analysis
Polysaccharides blood
Subjects
Details
- Language :
- English
- ISSN :
- 0264-6021
- Volume :
- 269
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- The Biochemical journal
- Publication Type :
- Academic Journal
- Accession number :
- 2390069
- Full Text :
- https://doi.org/10.1042/bj2690821