Article
Use of porcine fibrinogen as a model glycoprotein to study the binding specificity of the three variants of K88 lectin.
Infection and immunity - 1 May 1995
L'Hôte C, Berger S, Bourgerie S, Duval-Iflah Y, Julien R, Karamanos Y
Abstract excerpt
Known glycoproteins were used to determine the differences occurring in the binding specificities of the three variants of the K88 lectin in an approach essentially based on lectin blotting. During the screening, it was demonstrated that each variant of the K88 lectin biotinylated via its amino groups (NbioK88) exhibited a characteristic binding to the three chains of porcine fibrinogen. NbioK88ab weakly bound to...
Topics
- Animals
- Antigens, Bacterial
- Antigens, Surface
- Biotin
- Carbohydrate Sequence
- Escherichia coli Proteins
- Fibrinogen
- Fimbriae Proteins
- Fimbriae, Bacterial
- Genetic Variation
- Glycoproteins