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 ◽  
...  
1997 ◽  
Vol 2 (2) ◽  
pp. 218-224 ◽  
Author(s):  
Claudio O. Fernández ◽  
Oscar Podestá ◽  
Daniel A. Converso ◽  
Marcelo E. Fernández ◽  
A. J. Vila

2006 ◽  
Vol 23 (7-8) ◽  
pp. 591-598 ◽  
Author(s):  
Carlos Solórzano ◽  
Stéphane Bouquelet ◽  
M. Ali Pereyra ◽  
Francisco Blanco-Favela ◽  
Marie-Christine Slomianny ◽  
...  

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

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

1983 ◽  
Vol 3 (12) ◽  
pp. 2166-2171
Author(s):  
B Gilfix ◽  
J Rogers ◽  
B D Sanwal

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.


1982 ◽  
Vol 203 (1) ◽  
pp. 239-243 ◽  
Author(s):  
Willy J. Peumans ◽  
Hetty M. Stinissen ◽  
Albert R. Carlier

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.


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