Synthesis and Cholera Toxin Binding Properties of a Lactose-2-aminothiazoline Conjugate

2002 ◽  
Vol 4 (10) ◽  
pp. 1807-1808 ◽  
Author(s):  
Ioannis Vrasidas ◽  
Johan Kemmink ◽  
Rob M. J. Liskamp ◽  
Roland J. Pieters
Keyword(s):  
Cholera Toxin ◽  
Binding Properties ◽  
Toxin Binding

Short Term Neonatal Starvation Altered Cholera Toxin Binding in Rabbits

1989 ◽  
Vol 119 (2) ◽  
pp. 280-285
Author(s):  
Susan S. Baker ◽  
Cara Campbell ◽  
W. Allan Walker
Keyword(s):  
Cholera Toxin ◽  
Short Term ◽  
Toxin Binding

Identification of cholera toxin-binding sites in the nucleus of intestinal epithelial cells

FEBS Letters ◽  
1989 ◽  
Vol 242 (2) ◽  
pp. 309-313 ◽  
Author(s):  
Marianne E. Parkinson ◽  
Colin G. Smith ◽  
Peter B. Garland ◽  
Simon van Heyningen
Keyword(s):  
Epithelial Cells ◽  
Cholera Toxin ◽  
Binding Sites ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Toxin Binding

Strong inhibition of cholera toxin binding by galactose dendrimers

2007 ◽  
pp. 5043 ◽  
Author(s):  
Hilbert M. Branderhorst ◽  
Rob M. J. Liskamp ◽  
Gerben M. Visser ◽  
Roland J. Pieters
Keyword(s):  
Cholera Toxin ◽  
Strong Inhibition ◽  
Toxin Binding

scholarly journals Importance of Cry1 δ-Endotoxin Domain II Loops for Binding Specificity in Heliothis virescens(L.)

2001 ◽  
Vol 67 (1) ◽  
pp. 323-329 ◽  
Author(s):  
Juan Luis Jurat-Fuentes ◽  
Michael J. Adang
Keyword(s):  
Binding Sites ◽  
Heliothis Virescens ◽  
Brush Border Membrane ◽  
Membrane Vesicle ◽  
Membrane Vesicles ◽  
Cross Resistance ◽  
Binding Assays ◽  
Binding Properties ◽  
Toxin Binding ◽  
Cry Toxin

ABSTRACT We constructed a model for Bacillus thuringiensis Cry1 toxin binding to midgut membrane vesicles from Heliothis virescens. Brush border membrane vesicle binding assays were performed with five Cry1 toxins that share homologies in domain II loops. Cry1Ab, Cry1Ac, Cry1Ja, and Cry1Fa competed with 125I-Cry1Aa, evidence that each toxin binds to the Cry1Aa binding site in H. virescens. Cry1Ac competed with high affinity (competition constant [K com] = 1.1 nM) for 125I-Cry1Ab binding sites. Cry1Aa, Cry1Fa, and Cry1Ja also competed for125I-Cry1Ab binding sites, though theK com values ranged from 179 to 304 nM. Cry1Ab competed for 125I-Cry1Ac binding sites (K com = 73.6 nM) with higher affinity than Cry1Aa, Cry1Fa, or Cry1Ja. Neither Cry1Ea nor Cry2Aa competed with any of the 125I-Cry1A toxins. Ligand blots prepared from membrane vesicles were probed with Cry1 toxins to expand the model of Cry1 receptors in H. virescens. Three Cry1A toxins, Cry1Fa, and Cry1Ja recognized 170- and 110-kDa proteins that are probably aminopeptidases. Cry1Ab and Cry1Ac, and to some extent Cry1Fa, also recognized a 130-kDa molecule. Our vesicle binding and ligand blotting results support a determinant role for domain II loops in Cry toxin specificity for H. virescens. The shared binding properties for these Cry1 toxins correlate with observed cross-resistance in H. virescens.

Lectin and cholera toxin binding to guinea pig tumor (104C1) cell surfaces before and after glycosphingolipid incorporation

1976 ◽  
Vol 71 (1) ◽  
pp. 385-392 ◽  
Author(s):  
Manju Basu ◽  
Subhash Basu ◽  
William G. Shanabruch ◽  
Joseph R. Moskal ◽  
Charles H. Evans
Keyword(s):  
Guinea Pig ◽  
Cholera Toxin ◽  
Cell Surfaces ◽  
Toxin Binding ◽  
Before And After
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