Title : Studies on the oligosaccharide chains of human
alpha 1-protease inhibitor
Abstract :
- II
- Structure of oligosaccharides
- Human alpha 1-protease inhibitor has three oligosaccharide side chains attached to 3 separate asparaginyl residues of the protein by N-glycosyl linkages
- Two of the three asparaginyl residues link mostly to the A-type oligosaccharide chains which consist of Man3, Gal2, (GlcNAc)4 and (NeuAc)2
- One of the three asparaginyl residues also attaches to a B-type oligosaccharide chain, which consists of Man3, Gal3, (GlcNAc)5, and (NeuAc)3
- The ratio of A-chain to B-chain in this particular position is about 2:1
- The structures of A- and B-chains of the glycoprotein were examined by periodate oxidation, sequential glycosidase digestion, and permethylation
- The results unequivocally revealed the following structure for A-chains
- (Formula: see text)
- B-type oligosaccharide chains have an additional trisaccharide, i.e. NeuAc 2 alpha leads to 3 Gal 1 beta leads to 4 GlcNAc attached to mannose at the (a) and/or (b) position of A-type chains by a beta 1 leads to 4 linkage
- The sialic acid of human alpha 1-protease inhibitor was determined to be N-acetylneuraminic acid
Output (sent_index, trigger,
protein,
sugar,
site):
- 0. alpha, , alpha 1-protease inhibitor, the oligosaccharide chains, -
- 10. position, , -, mannose, position
- 11. inhibitor, , alpha 1-protease inhibitor, N-acetylneuraminic acid, -
- 11. inhibitor, , alpha 1-protease inhibitor, The sialic acid, -
- 3. attached, , protein, three oligosaccharide side chains, residues
- 3. has, , Human alpha 1-protease inhibitor, three oligosaccharide side chains, -
- 7. glycoprotein, , glycoprotein, -, -
Output(Part-Of) (sent_index,
protein,
site):
*Output_Site_Fusion* (sent_index,
protein,
sugar,
site):