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

Pesliakas, Henrikas; Žutautas, Vilius; Baškevičiūt≐, Birut≐

doi:10.1016/0021-9673(94)87070-5

Cited by 9 publications

(1 citation statement)

References 28 publications

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“…It was established that lactate dehydrogenase showed a higher affinity when it interacted with dyes without Cu 2+ ions in their structure. The same group (Pesliakas et al, 1994) Otto et al (1993) investigated the surface of lactate dehydrogenase isoenzymes from different species for the presence of metal chelate binding sites. Kwon et al (1999) used Sepharose 4B as ligand carrier for metal ion affinity partitioning of protein in PEG/dextran aqueous two-phase systems.…”

Section: Metal Ions Affinity Partitioningmentioning

confidence: 99%

Liquid-liquid extraction of enzymes by affinity aqueous two-phase systems

Souza

Pontes

et al. 2003

Braz. arch. biol. technol.

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From analytical to commercial scale, aqueous two-phase systems have their application in the purification, characterization and study of biomaterials. In order to improve the selectivity of the systems, the biospecific affinity ligands were introduced. In the affinity partitioning aqueous two-phase system, have many enzymes been purified. This review discusses the partitioning of some enzymes in the affinity aqueous two-phase systems in regard to the different ligands, including reactive dyes, metal ions and other ligands. Some integration of aqueous two-phasesystem with other techniques for more effective purification of enzymes are also presented.

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Section: Metal Ions Affinity Partitioningmentioning

confidence: 99%

Liquid-liquid extraction of enzymes by affinity aqueous two-phase systems

Souza

Pontes

et al. 2003

Braz. arch. biol. technol.

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Immobilized metal ion affinity chromatography: a review on its applications

Cheung

Wong

2012

Appl Microbiol Biotechnol

211

145

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After 35 years of development, immobilized metal ion affinity chromatography (IMAC) has evolved into a popular protein purification technique. This review starts with a discussion of its mechanism and advantages. It continues with its applications which include the purification of histidine-tagged proteins, natural metal-binding proteins, and antibodies. IMAC used in conjunction with mass spectroscopy for phosphoprotein fractionation and proteomics is also covered. Finally, this review addresses the developments, limitations, and considerations of IMAC in the biopharmaceutical industry.

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