Evaluation of monoclonal anti-A and anti-B and affinity-purified Ulex europaeus lectin I for forensic blood grouping

1984 ◽  
Vol 93 (4) ◽  
Author(s):  
R.E. Gaensslen ◽  
H.C. Lee ◽  
J.E. Carroll
Keyword(s):  
Ulex Europaeus ◽  
Blood Grouping ◽  
Ulex Europaeus Lectin I

Examination of the structural basis for O(H) blood group specificity by Ulex europaeus Lectin I

2002 ◽  
Vol 80 (8) ◽  
pp. 1010-1021 ◽  
Author(s):  
Gerald F Audette ◽  
Douglas J Olson ◽  
Andrew R Ross ◽  
J Wilson Quail ◽  
Louis T Delbaere
Keyword(s):  
Blood Group ◽  
Structural Basis ◽  
Carbohydrate Recognition ◽  
X Ray ◽  
Ulex Europaeus ◽  
Cell Dimensions ◽  
Unit Cell Dimensions ◽  
Ulex Europaeus Lectin I

The structural basis for carbohydrate specificity of the first lectin from Ulex europaeus (UE-I) is reported. UE-I is a dimeric metalloglycoprotein that binds the H-type 2 human blood group determinant (α-L-Fucα(1[Formula: see text]2)-β;-D-Galβ(1[Formula: see text]4)-β-D-GlcNAcα-), the blood group determinant present on the surface of O-type erythrocytes. The structural characteristics of UE-I involved in carbohydrate recognition have been examined using mass spectrometry (MS) and X-ray diffraction analysis. MS analysis allowed for discrimination between the different primary structures reported for UE-I. To examine the binding of the H-type 2 blood group determinant by UE-I, the methyl glycosides of the fucose monosaccharide (α-L-Fuc-OMe), known to exhibit primary binding specificity, and the H-type 2 trisaccharide (H-type 2-OMe) were, in two separate experiments, co-crystallized into the binding site of UE-I. The UE-I:α-L-Fuc-OMe complex crystallizes in the monoclinic space group P21, with unit cell dimensions a = 71.81, b = 69.00, and c = 119.02 Å, and β = 106.76°. Two UE-I dimers are observed to be present within the asymmetric unit, and the model has been refined to a R-value and RFree of 0.202 and 0.289, respectively, to 2.3 Å resolution. The preliminary model of the UE-I:H-type 2-OMe complex has been refined at 3.0 Å resolution. The UE-I:H-type 2-OMe complex crystallizes in the orthorhombic space group C2221, with unit cell dimensions a = 88.80, b = 164.75, and c = 77.42 Å, and a single UE-I dimer is present within the asymmetric unit. The carbohydrate recognition domain of UE-I has been identified to be comprised of residues Glu44, Thr86, Asp87, Arg102, Ala103, Gly104, Gly105, Tyr106, Ile129, Val133, Asn134, Trp136, Tyr219, and Arg222. Several critical protein-carbohydrate interactions have been identified, including the role of the hydrophobic interaction between the Thr86 side chain and C-5-CH3 of the α-L-Fuc-OMe. The role of these interactions in carbohydrate recognition-binding by UE-I, as well as differences between the observed and previously modeled complexes, are discussed. Key words: Ulex europaeus lectin I, H-type 2 human blood group determinant, protein-carbohydrate interactions, X-ray crystallography, chemical mapping.

P 15 Ulex europaeus lectin I-enzyme conjugates for H substance ELISA

1983 ◽  
Vol 23 (1) ◽  
pp. 75-76
Author(s):  
Patricia W. Harris-Smith ◽  
S.M. Fletcher
Keyword(s):  
Ulex Europaeus ◽  
Ulex Europaeus Lectin I

Knowledge-based modeling of a legume lectin and docking of the carbohydrate ligand: The Ulex europaeus lectin I and its interaction with fucose

1996 ◽  
Vol 14 (6) ◽  
pp. 322-327 ◽  
Author(s):  
Arnaud Gohier ◽  
Juan Felix Espinosa ◽  
Jesus Jimenez-Barbero ◽  
Pierre-Alain Carrupt ◽  
Serge Pérez ◽  
...  
Keyword(s):  
Ulex Europaeus ◽  
Knowledge Based ◽  
Legume Lectin ◽  
Carbohydrate Ligand ◽  
Ulex Europaeus Lectin I

Binding sites of Ulex europaeus-lectin I in human parotid gland

1987 ◽  
Vol 248 (2) ◽  
Author(s):  
I.Antonio Born ◽  
Klaus-P. Zimmer ◽  
Karl Schwechheimer ◽  
Heinz Maier ◽  
Peter M�ller
Keyword(s):  
Parotid Gland ◽  
Binding Sites ◽  
Ulex Europaeus ◽  
Human Parotid Gland ◽  
Ulex Europaeus Lectin I

Crystallization of Ulex europaeus Lectin I

1994 ◽  
Vol 243 (2) ◽  
pp. 345-346 ◽  
Author(s):  
Margaret Vandonselaar ◽  
Louis T.J. Delbaere
Keyword(s):  
Ulex Europaeus ◽  
Ulex Europaeus Lectin I

scholarly journals Binding of human liver hydrolases by immobilized lectins

1979 ◽  
Vol 177 (1) ◽  
pp. 175-180 ◽  
Author(s):  
M B Fiddler ◽  
Y Ben-Yoseph ◽  
H L Nadler
Keyword(s):  
Human Liver ◽  
Similar Data ◽  
Galactosidase Activity ◽  
Purification And Characterization ◽  
Ulex Europaeus ◽  
Glucuronidase Activity ◽  
Beta Galactosidase ◽  
Carbohydrate Specificities ◽  
Ulex Europaeus Lectin I

The binding of 22 human liver hydrolase activities by immobilized lectins of six different carbohydrate specificities, namely alpha-D-mannose (glucose), D-N-acetylglucosamine, D-N-acetylgalactosamine, L-fucose, alpha-D-galactose and beta-D-galactose, were examined. Differences in binding among these enzymes and within specific enzymes were observed. For example, the neutral forms of alpha-mannosidase and beta-xylosidase were bound by the Ulex europaeus lectin I (specific for L-fucose), whereas the acidic forms were not. Bandierea simplicifolia lectin (specific for alpha-galactose) bound 65% of beta-glucuronidase activity; recycling experiments demonstrated complete binding of the enzyme that had been eluted with the competitor D-galactose and no binding of the fraction that was not initially bound. These results suggested the presence of two forms of this enzyme. Similar data were obtained for acidic beta-galactosidase activity. These experiments may provide the basis for the expanded use of immobilized lectins for purification and characterization of hydrolases and other glycoproteins.

ABO Blood Grouping of Human Hair by Universal Immuno-Peroxidase Polymer (UIP) Technique

2003 ◽  
Vol 7 (2) ◽  
pp. 145-153
Author(s):  
Yasunari Hisashi ◽  
Tatsuo Shinozuka ◽  
Osamu Ohue ◽  
Setsuko Takei ◽  
Ayako Ro ◽  
...  
Keyword(s):  
Human Hair ◽  
Abo Blood Grouping ◽  
Blood Grouping

Blood-grouping

BMJ ◽  
1956 ◽  
Vol 1 (4965) ◽  
pp. 514-515
Author(s):  
R. Drummond
Keyword(s):  
Blood Grouping
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