Characterization of Wheat Germ Agglutinin Ligand on Soluble Glycoproteins in Caenorhabditis elegans

2005 ◽  
Vol 138 (2) ◽  
pp. 209-213 ◽  
Author(s):  
Shunji Natsuka ◽  
Masahumi Kawaguchi ◽  
Yukiko Wada ◽  
Akira Ichikawa ◽  
Koji Ikura ◽  
...  
Keyword(s):  
Caenorhabditis Elegans ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ

Bacterial expression, purification and biophysical characterization of wheat germ agglutinin and its four hevein-like domains

Biopolymers ◽  
2018 ◽  
Vol 110 (1) ◽  
pp. e23242 ◽  
Author(s):  
Eduardo Leyva ◽  
Jorge L. Medrano-Cerano ◽  
Patricia Cano-Sánchez ◽  
Itzel López-González ◽  
Homero Gómez-Velasco ◽  
...  
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Bacterial Expression ◽  
Biophysical Characterization

Isolation and characterization of the potential receptor for wheat germ agglutinin from human neutrophils

2006 ◽  
Vol 23 (7-8) ◽  
pp. 591-598 ◽  
Author(s):  
Carlos Solórzano ◽  
Stéphane Bouquelet ◽  
M. Ali Pereyra ◽  
Francisco Blanco-Favela ◽  
Marie-Christine Slomianny ◽  
...  
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Human Neutrophils ◽  
Isolation And Characterization

scholarly journals Characterization of the wheat germ agglutinin binding to self-assembled monolayers of neoglycoconjugates by AFM and SPR

Glycobiology ◽  
2009 ◽  
Vol 19 (6) ◽  
pp. 633-643 ◽  
Author(s):  
Michael Lienemann ◽  
Arja Paananen ◽  
Harry Boer ◽  
Jesús M de la Fuente ◽  
Isabel García ◽  
...  
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Self Assembled Monolayers ◽  
Assembled Monolayers ◽  
Self Assembled

Isolation and characterization of rat skeletal myoblast mutants resistant to lectins

1983 ◽  
Vol 3 (12) ◽  
pp. 2166-2171
Author(s):  
B Gilfix ◽  
J Rogers ◽  
B D Sanwal
Keyword(s):  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Wild Type ◽  
Skeletal Myoblast ◽  
Skeletal Myoblasts ◽  
Isolation And Characterization ◽  
Low Concentrations ◽  
High Concentrations ◽  
Made In

Mutants resistant to the lethal action of the lectins phytohemagglutinin A (PHA) and wheat germ agglutinin (WGA) have been made in a line of differentiating rat skeletal myoblasts. The WGA mutants are of two types, WGArII, resistant to low concentrations of the lectin, and WGArI, resistant to high concentrations of the lectin. WGArII and PHAr mutants are unable to differentiate, whereas WGArI mutants differentiate normally. WGArII mutants are not impaired in the binding of wheat germ agglutinin, but WGArI mutants bind the lectin only to the extent of about 50% of the wild-type values. All of the mutants are cross-resistant to lectins other than those used in their selection.

scholarly journals Isolation and partial characterization of wheat-germ-agglutinin-like lectins from rye (Secale cereale) and barley (Hordeum vulgare) embryos

1982 ◽  
Vol 203 (1) ◽  
pp. 239-243 ◽  
Author(s):  
Willy J. Peumans ◽  
Hetty M. Stinissen ◽  
Albert R. Carlier
Keyword(s):  
Hordeum Vulgare ◽  
Affinity Chromatography ◽  
Secale Cereale ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Partial Characterization ◽  
Immunological Properties

Lectins have been isolated from embryos of Secale cereale (rye) and Hordeum vulgare (barley) by affinity chromatography on immobilized N-acetylglucosamine. Both lectins are dimeric proteins of two identical subunits of mol.wt. 18000. They resemble strongly wheat-germ agglutinin with respect to their chemical, physical, biological and immunological properties.

scholarly journals Isolation and partial characterization of a lectin from a false brome grass (Brachypodium sylvaticum)

1982 ◽  
Vol 205 (3) ◽  
pp. 635-638 ◽  
Author(s):  
W J Peumans ◽  
C Spaepen ◽  
H M Stinissen ◽  
A R Carlier
Keyword(s):  
Physicochemical Properties ◽  
Affinity Chromatography ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Partial Characterization ◽  
Grass Species ◽  
Brachypodium Sylvaticum ◽  
Dimeric Protein ◽  
Brome Grass

A lectin has been isolated from embryos of a false brome grass species (Brachypodium sylvaticum) by affinity chromatography on immobilized N-acetylglucosamine. It is a dimeric protein of two identical subunits of mol.wt. 18 000. Although it resembles cereal lectins with respect to its biochemical and physicochemical properties, it differs structurally in several aspects from wheat-germ-agglutinin-like lectins.

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