Purification of diphtheria toxin by chromatography on Cibacron Blue-Sepharose.
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.
D000873:Anthracenes; D002846:Chromatography, Affinity / Q000379:methods; D004396:Coloring Agents; D004167:Diphtheria Toxin / Q000302:isolation & purification*; D006801:Humans; D012685:Sepharose / Q000031:analogs & derivatives; D012709:Serum Albumin; D013053:Spectrophotometry
D000873:Anthracenes; D004396:Coloring Agents; D004167:Diphtheria Toxin; D012709:Serum Albumin; C017842:cibacron blue-sepharose; D012685:Sepharose