In:
European Journal of Biochemistry, Wiley, Vol. 205, No. 3 ( 1992-05), p. 961-978
Abstract:
The carbohydrate side chains of the thrombin‐like serine protease ancrod from the venom of the Malayan pit viper Agkistrodon rhodostoma were liberated from tryptic glycopeptides by treatment with peptide‐ N 4 ‐( N ‐acetyl‐β‐glucosaminyl)asparagine amidase F and fractionated by high‐performance liquid chromatography. Glycans obtained were characterized by digestion with exoglycosidases, methylation analysis and, in part, by liquid secondary‐ion mass spectrometry and 1 H‐NMR spectroscopy. The results reveal that this snake venom glycoprotein contains partially truncated di‐, tri‐ and tetraantennary complex type N ‐glycans carrying Fuc(α1‐6) residues at the innermost N ‐ acetylglucosamine and solely (α2‐3)‐linked sialic acid substituents. As a characteristic feature, ancrod oligosaccharides comprise mainly sialylated Galβ3GlcNAcβ lactosamine antennae. Furthermore, a small proportion of the sugar chains were found to carry a NeuAcα3GalNAcβ4GlcNAcβ antenna exclusively linked to C‐2 of Man(α1‐3) residues of the pentasaccharide core. Thus, many of the glycans found represent novel glycoprotein‐ N ‐glycan structures.
Type of Medium:
Online Resource
ISSN:
0014-2956
,
1432-1033
DOI:
10.1111/ejb.1992.205.issue-3
DOI:
10.1111/j.1432-1033.1992.tb16863.x
Language:
English
Publisher:
Wiley
Publication Date:
1992
detail.hit.zdb_id:
1398347-7
detail.hit.zdb_id:
1464377-7
SSG:
12
Permalink