Purification of diphtheria toxin by chromatography on Cibacron Blue-Sepharose
- 1 August 1983
- journal article
- Published by Springer Nature in Cellular and Molecular Life Sciences
- Vol. 39 (8) , 885-886
- https://doi.org/10.1007/bf01990419
Abstract
Diphtheria toxin binds to Cibacron Blue-Agarose and may be eluted by increasing the ionic strength of the elution buffer. Experiments using difference spectroscopy showed that the interaction between toxin and dye is ionic rather than hydrophobic, and therefore it is of a different nature with respect to that usually found in nucleotide-requiring enzymes.Keywords
This publication has 10 references indexed in Scilit:
- Different interactions of human and bovine serum albumin with Cibacron Blue and Blue Dextran.1982
- Ligand interactions of diphtheria toxin. I. Binding and hydrolysis of NAD.Journal of Biological Chemistry, 1980
- Dihydrofolate reductases from chicken liver and Lactobacillus casei bind Cibacron blue F3GA in different modes and at different sites.Journal of Biological Chemistry, 1980
- Use of blue dextran as a probe for the Nicotinamide Adenine Dinucleotide domain in proteinsAccounts of Chemical Research, 1977
- Diphtheria toxin: mode of action and structure.1975
- Diphtheria toxin: mode of action and structureMicrobiology and Molecular Biology Reviews, 1975
- Affinity chromatography purification of diphtheria toxinBiotechnology & Bioengineering, 1974
- Structure and activity of diphtheria toxin. II. Attack by trypsin at a specific site within the intact toxin molecule.1971
- Structure and Activity of Diphtheria ToxinPublished by Elsevier ,1971
- Quantitative estimation of proteins by electrophoresis in agarose gel containing antibodiesAnalytical Biochemistry, 1966