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
Output (sent_index, trigger,
protein,
sugar,
site):
- 3. lactotransferrin, , lactotransferrin, the glycans, -
- 3. lactotransferrin, , lactotransferrin, the molar carbohydrate compositions, -
- 4. disialylated, , -, two disialylated and non-fucosylated biantennary glycans, -
- 4. non-fucosylated, , -, two disialylated and non-fucosylated biantennary glycans, -
- 4. released, , lactotransferrin, oligosaccharide alditols, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):