Title : Primary structure of
glycans isolated from human leucocyte
lactotransferrin
Abstract :
- Absence of fucose residues questions the proposed mechanism of hyposideraemia
- 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