Metal ion-promoted binding of proteins to immobilized triazine dye affinity adsorbents

Biochim Biophys Acta. 1982 Jan 4;700(1):90-100. doi: 10.1016/0167-4838(82)90296-5.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alkaline Phosphatase / metabolism*
  • Carboxypeptidases / metabolism*
  • Cations, Divalent
  • Chelating Agents
  • Coloring Agents
  • Enzymes, Immobilized / metabolism*
  • Hexokinase / metabolism*
  • Metals / pharmacology*
  • Ovalbumin / metabolism*
  • Protein Binding
  • Triazines
  • gamma-Glutamyl Hydrolase / metabolism*


  • Cations, Divalent
  • Chelating Agents
  • Coloring Agents
  • Enzymes, Immobilized
  • Metals
  • Triazines
  • Ovalbumin
  • Hexokinase
  • Alkaline Phosphatase
  • Carboxypeptidases
  • gamma-Glutamyl Hydrolase