The synthesis and lectin-binding properties of novel mannose-functionalised polymers

RSC Advances ◽  
2013 ◽  
Vol 3 (35) ◽  
pp. 15435 ◽  
Author(s):  
Hayley Charville ◽  
Jianyong Jin ◽  
Clive W. Evans ◽  
Margaret A. Brimble ◽  
David E. Williams
Keyword(s):  
Lectin Binding ◽  
Binding Properties

Leguminous glycosidases: Hydrophobic and lectin binding properties

1989 ◽  
Vol 28 (2) ◽  
pp. 355-357 ◽  
Author(s):  
Wolfgang Einhoff ◽  
Harold Rüdiger
Keyword(s):  
Lectin Binding ◽  
Binding Properties

Newly established human pancreatic carcinoma cell lines and their lectin binding properties

1993 ◽  
Vol 13 (1) ◽  
pp. 31-41
Author(s):  
Nobuyuki Nishimura ◽  
Seiji Saito ◽  
Yoshiki Kubota ◽  
Nan-yo Moto-o ◽  
Kuniko Taguchi ◽  
...  
Keyword(s):  
Pancreatic Carcinoma ◽  
Cell Lines ◽  
Carcinoma Cell ◽  
Lectin Binding ◽  
Binding Properties ◽  
Carcinoma Cell Lines ◽  
Human Pancreatic Carcinoma Cell

Peanut lectin binding properties of germinal centers of mouse lymphoid tissue

Nature ◽  
1980 ◽  
Vol 284 (5754) ◽  
pp. 364-366 ◽  
Author(s):  
M. L. Rose ◽  
M. S. C. Birbeck ◽  
V. J. Wallis ◽  
J. A. Forrester ◽  
A. J. S. Davies
Keyword(s):  
Lymphoid Tissue ◽  
Lectin Binding ◽  
Germinal Centers ◽  
Peanut Lectin ◽  
Binding Properties

scholarly journals Fine specificity of domain-I of recombinant tandem-repeat-type galectin-4 from rat gastrointestinal tract (G4-N)

2002 ◽  
Vol 367 (3) ◽  
pp. 653-664 ◽  
Author(s):  
Albert M. WU ◽  
June H. WU ◽  
Ming-Sung TSAI ◽  
Jia-Hau LIU ◽  
Sabine ANDRÉ ◽  
...  
Keyword(s):  
Blood Group ◽  
Lectin Binding ◽  
Binding Properties ◽  
Lectin Domain ◽  
Cell Matrix ◽  
Endogenous Lectins ◽  
Differential Binding ◽  
Definition Of ◽  
Domain I ◽  
Blood Group Abh

Galectins, a family of β-galactoside-specific endogenous lectins, are involved in regulating diverse activities such as proliferation/apoptosis, cell—cell (matrix) interaction and cell migration. It is presently unclear to what extent the carbohydrate fine specificities of the combining sites of mammalian galectins overlap. To address this issue, we performed an analysis of the carbohydrate-recognition domain (CRD-I) near the N-terminus of recombinant rat galectin-4 (G4-N) by the biotin/avidin-mediated microtitre plate lectin-binding assay with natural glycoproteins (gps)/polysaccharide and by the inhibition of galectin—glycan interactions with a panel of glycosubstances. Among the 35 glycans tested for lectin binding, G4-N reacted best with human blood group ABH precursor gps, and asialo porcine salivary gps, which contain high densities of the blood group Ii determinants Galβ1-3GalNAc (the mucin-type sugar sequence on the human erythrocyte membrane) and/or GalNAcα1-Ser/Thr (Tn), whereas this lectin domain reacted weakly or not at all with most sialylated gps. Among the oligosaccharides tested by the inhibition assay, Galβ1-3GlcNAcβ1-3Galβ1-4Glc was the best. It was 666.7 and 33.3 times more potent than Gal and Galβ1-3GlcNAc, respectively. G4-N has a preference for the β-anomer of Gal at the non-reducing ends of oligosaccharides with a Galβ1-3 linkage, over Galβ1-4 and Galβ1-6. The fraction of Tn glycopeptide from asialo ovine submandibular glycoprotein was 8.3 times more active than Galβ1-3GlcNAc. The overall carbohydrate specificity of G4-N can be defined as Galβ1-3GlcNAcβ1-3Galβ1-4Glc (lacto-N-tetraose)>Galβ1-4GlcNAcβ1-3Galβ1-4Glc (lacto-N-neo-tetraose) and Tn clusters>Galβ1-4Glc and GalNAcβ1-3Gal>Galβ1-3GalNAc>Galβ1-3GlcNAc>Galβ1-4GlcNAc>GalNAc>Gal. The definition of this binding profile provides the basis to detect differential binding properties relative to the other galectins with ensuing implications for functional analysis.

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