Metal ion-promoted binding of proteins to immobilized triazine dye affinity adsorbents.
Low concentrations of metal ions, particularly those of the first row transition series such as Zn2+, Co2+, Mn2+, Ni2+, Cu2+, and, to a lesser extent, the group IIA ions, Ca2+ and Mg2+, promotes binding of carboxypeptidase G2, alkaline phosphatase and yeast hexokinase to immobilized Procion Red H-8BN, Procion Yellow H-A and Cibacron Blue F3G-A respectively. The binding of ovalbumin to immobilized Cibacron Blue F3G-A and Procion Orange MX-G is selectively enhanced in the presence of AI3+. With ovalbumin and alkaline phosphatase, the effect is almost totally specific for both the metal ion and dye, whereas with carboxypeptidase G2 and hexokinase, metal ions such as Co2+, Ni2+, Mn2+, Cu2+, Ca2+ and Mg2+ also promote binding to varying degrees. Almost all other monovalent and trivalent metal ions appear to be ineffective. Metal ion-bound enzymes can subsequently be eluted with appropriate chelating agents of the amine, aminocarboxylate or substituted pyridine classes.
D000469:Alkaline Phosphatase / Q000378:metabolism*; D002268:Carboxypeptidases / Q000378:metabolism*; D002413:Cations, Divalent; D002614:Chelating Agents; D004396:Coloring Agents; D004800:Enzymes, Immobilized / Q000378:metabolism*; D006593:Hexokinase / Q000378:metabolism*; D008670:Metals / Q000494:pharmacology*; D010047:Ovalbumin / Q000378:metabolism*; D011485:Protein Binding; D014227:Triazines; D011623:gamma-Glutamyl Hydrolase / Q000378:metabolism*
D002413:Cations, Divalent; D002614:Chelating Agents; D004396:Coloring Agents; D004800:Enzymes, Immobilized; D008670:Metals; D014227:Triazines; D010047:Ovalbumin; D006593:Hexokinase; D000469:Alkaline Phosphatase; D002268:Carboxypeptidases; D011623:gamma-Glutamyl Hydrolase