Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains

A A Bergwerff; J E Thomas-Oates; J van Oostrum; J P Kamerling; J F Vliegenthart

doi:10.1016/0014-5793(92)81512-k

Human urokinase contains GalNAc beta (1-4)[Fuc alpha (1-3)]GlcNAc beta (1-2) as a novel terminal element in N-linked carbohydrate chains

FEBS Lett. 1992 Dec 21;314(3):389-94. doi: 10.1016/0014-5793(92)81512-k.

Authors

A A Bergwerff¹, J E Thomas-Oates, J van Oostrum, J P Kamerling, J F Vliegenthart

Affiliation

¹ Bijvoet Center, Department of Bio-Organic Chemistry, Utrecht University, The Netherlands.

PMID: 1468573
DOI: 10.1016/0014-5793(92)81512-k

Abstract

Structural analysis of enzymically released N-linked carbohydrate chains of human urokinase (urinary-type plasminogen activator) by 1H NMR spectroscopy and FAB-MS demonstrated that the N-linked oligosaccharides on the only N-glycosylation site contain diantennary structures with the novel GalNAc beta (1-4) [Fuc alpha (1-3)]GlcNAc beta (1-2) element in the upper or the lower branch.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Carbohydrate Sequence
Humans
Magnetic Resonance Spectroscopy
Molecular Sequence Data
Spectrometry, Mass, Fast Atom Bombardment
Urokinase-Type Plasminogen Activator / chemistry*

Substances

Urokinase-Type Plasminogen Activator