Chemical Modifications of the Toxic Lectins Abrin and Ricin
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1978.tb12171.x/fullpdf
Reference29 articles.
1. 1. S. Olsnes, A. Pihl, and P. Cuatrecasas (1976 ) inReceptors and Recognition Series B: The Specificity and Action of Animal, Bacterial and Plant Toxins () pp.129 -173 , Chapman and Hall, London.
2. Abrin and Ricin: New Anti-tumour Substances
3. Isolation and Properties of Abrin: a Toxic Protein Inhibiting Protein Synthesis. Evidence for Different Biological Functions of Its Two Constituent-Peptide Chains
4. Different biological properties of the two constituent peptide chains of ricin a toxic protein inhibiting protein synthesis
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2. AB-type lectin (toxin/agglutinin) from mistletoe: differences in affinity of the two galactoside-binding Trp/Tyr-sites and regulation of their functionality by monomer/dimer equilibrium;Glycobiology;2006-06-14
3. Monomer/dimer equilibrium of the AB-type lectin from mistletoe enables combination of toxin/agglutinin activities in one protein: analysis of native and citraconylated proteins by ultracentrifugation/gel filtration and cell biological consequences of dimer destabilization;Glycobiology;2005-07-21
4. Purification, some properties of a D-galactose-binding leaf lectin from Erythrina indica and further characterization of seed lectin;Biochimie;2002-10
5. Reduction of Ricin Toxicity without Impairing the Saccharide-Binding Properties by Chemical Modification of the Carboxyl Groups;Analytical Biochemistry;1993-02
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