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Immobilized metal-ion affinity partitioning of NAD+-dependent dehydrogenases in poly(ethylene glycol)-dextran two-phase systems

Authors
Journal
Journal of Chromatography A
0021-9673
Publisher
Elsevier
Publication Date
Volume
678
Issue
1
Identifiers
DOI: 10.1016/0021-9673(94)87070-5
Disciplines
  • Biology

Abstract

Abstract Affinity partitioning of yeast alcohol dehydrogenase (YADH), lactate dehydrogenase from rabbit muscle (MLDH) and lactate and malate dehydrogenases from pig heart (HLDH and HMDH, respectively) were studied in aqueous two-phase systems containing metal ions (Cu 2+, Ni 2+, Zn 2+ and Cd 2+) chelated by iminodiacetate-poly(ethylene glycol) (IDA-PEG). The partitioning behaviour of the enzymes in the presence of Cu(II)-IDA-PEG was studied as a function of the concentration of NaCl, the pH of the medium and the concentration of added selected agents. It was demonstrated that the partition effect (Δ log K) of dehydrogenases in the presence of Cu(II)-IDA-PEG and the affinity of enzymes for immobilized Cu 2+ ions increases in the order MLDH > YADH > HMDH ⩾ HLDH. It was shown that the determined variations in the enzyme affinities for Cu(II)-IDA-PEG might be related to the differences in the content of histidine residues accessible to the solvent.

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