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DOI: 10.1055/s-0038-1650648
O-glycosylation of Fibrinogen from Different Mammalian Species as Revealed by the Binding of Escherichia coli Biotinylated Lectins
Publication History
Received 19 April 1996
Accepted after revision 25 July 1996
Publication Date:
11 July 2018 (online)
![](https://www.thieme-connect.de/media/10.1055-s-00035024/199605/lookinside/thumbnails/10-1055-s-0038-1650648-1.jpg)
Summary
After the demonstration that neither N-glycans nor neuraminic acid are involved in the binding of K88 lectins to the Bp and y chains of porcine fibrinogen and that their recognition was due to O-glycans (L’Hôte C, Berger S, Bourgerie S, Duval-Iflah Y, Julien R, Karamanos Y. Infect Immun 1995; 63: 1927-1932) it clearly appeared that these lectins could be used as probes to detect O-glycans on fibrinogens of other species. The conclusion of the present study is that many mammalian fibrinogens contain complex O-glycans on βp and γ chains. In addition, the combined use of the biotinylated K99 lectin and the Peanut agglutinin demonstrated the presence of sialylated T-antigens on the A± chains of all the fibrinogens examined. These lectins can now be used to determine differences on the glycosylation status of fibrinogens within one species and also to detect O-glycans on other glycoproteins
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