Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:1.1.1.1 (alcohol dehydrogenase)
 9,284 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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 (Cu2+, Ni2+, Zn2+ and Cd2+) 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 (delta log K) of dehydrogenases in the presence of Cu(II)-IDA-PEG and the affinity of enzymes for immobilized Cu2+ ions increases in the order MLDH > YADH > HMDH > or = 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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PMID:Immobilized metal-ion affinity partitioning of NAD(+)-dependent dehydrogenases in poly(ethylene glycol)-dextran two-phase systems. 752 41

The optimization of a chromatographic process using immobilized metal affinity chromatography requires an understanding of the factors that govern the interaction between proteins and immobilized metal ions. Factors, such as concentrations of protein, NaCl and imidazole were investigated to elucidate kinetics of adsorption of alcohol dehydrogenase (ADH) onto a dye-iminodiacetic acid matrix (dye-IDA matrix). The results indicate that the adsorption of ADH onto a dye-IDA matrix occurs in the mode of multiple-site binding interactions between ADH and zinc ions immobilized on the dye-IDA matrix. The estimated average number of interaction sites was 4.5 and the association constant was 6 x 10(-9) mM(-n). The isotherm of ADH adsorption was well represented by a multivalent model of protein-zinc ion interactions. For the adsorption of ADH from clarified yeast homogenate, addition of imidazole as a protein competitor to adsorption buffer increased the adsorption specificity of ADH, thereby suppressing contaminant protein adsorption. It was also observed that the adsorption of ADH was better performed at high initial protein concentrations in the yeast homogenate. Consequently, these results may have important implications on the optimization of the strategy for immobilized metal affinity adsorption in packed and expanded bed systems.
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PMID:Multivalent binding interaction of alcohol dehydrogenase on dye-metal affinity matrix. 1623 3