Disease relevance of Thiodigalactoside

• Microcalorimetric study of the binding of thiodigalactoside to the lactose permease M protein of Escherichia coli [1].

High impact information on Thiodigalactoside

• However, all of the lectins competed for the same binding sites on rabbit erythrocytes, and could be inhibited by the same saccharide haptens (notably lactose and thiodigalactoside) [2].
• The results indicate a preference of the lectin for nonreducing beta-linked d-Gal residues being the best inhibitors of red blood cells binding methyl-beta-d-Gal and thiodigalactoside (Gal beta 1-4-thiogalactopyranoside) [3].
• Ligand thiodigalactoside protection against alkylation of the Cys-148 residue in the permease shows proper post-translational insertion [4].
• In the current study, 14 independent lactose permease mutants were isolated from the Val177/Asn319 parent which were resistant to thiodigalactoside growth inhibition but retained the ability to transport maltose [5].
• Under some experimental conditions, thiodigalactoside, the most potent inhibitor of lectin activity, inhibited the aggregation of cells of the extra-embryonic endoderm of the primitive chick embryo [6].

Biological context of Thiodigalactoside

• Transformation of this recombinant plasmid into Escherichia coli BL21 DE3 cells containing the T7 RNA polymerase, under the control of the lac UV5 promoter, allows expression of the subunit on induction of the T7 RNA polymerase by isopropyl thiodigalactoside [7].
• The enhanced cell growth was inhibited by thiodigalactoside (TDG, a potent inhibitor of beta-galactoside binding) and GAL1 monoclonal antibodies, suggesting GAL1's specific effect on the proliferation of 3T3 cells upon chitosan membranes [8].
• Thiodigalactoside binding lectin and skeletal myogenesis [9].

Anatomical context of Thiodigalactoside

• Although a thiodigalactoside binding lectin is present in extracts of developing myoblasts, it is also present in equivalent amounts in developmentally defective nonfusing variants [9].
• Cells from the extraembryonic endoderm of the gastrulating chick embryo contain a beta-D-galactoside-binding lectin inhibited by thiodigalactoside (TDG) [10].
• TDG-treated neurites are less well spread out than the controls; fascicle diameters and lengths are not altered [11].

Associations of Thiodigalactoside with other chemical compounds

• Reactions were essentially enthalpically driven with the binding enthalpies ranging from -53.8 kJ/mol for thiodigalactoside at 301 K to -2.2 kJ/mol for galactose at 300 K, indicating that hydrogen-bonding and van der Waals interactions provide the major stabilization for these reactions [12].
• The early heart anlagen of Xenopus laevis embryos were exposed to purified embryonic galactoside-binding lectin or its potent hapten inhibitor thiodigalactoside (TDG) [13].

Gene context of Thiodigalactoside

• The results show that lactose and thiodigalactoside were two of the best inhibitors of CBP binding to asialofetuin [14].

Analytical, diagnostic and therapeutic context of Thiodigalactoside

• Defective development of the craniofacial/digestive complex of Xenopus laevis after treatment with endogenous galactoside-binding lectin or its hapten inhibitor thiodigalactoside [15].

References