Copper(II)-iminodiacetic acid chelating resin as a stationary phase in the immobilized metal ion affinity chromatography of some aromatic amines

Liu, Yu; Yu, Shilin

doi:10.1016/s0021-9673(01)89310-9

Cited by 7 publications

(2 citation statements)

References 14 publications

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“…The transition metals can form stable complexes with electron-rich compounds and may coordinate molecules containing oxygen (O), nitrogen (N), and sulfur (S) by ion dipole interactions and dative bond formation (Porath et al., 1975). IMAC applications have been used in separation of amino acids, nucleotides, and small molecules such as amines and in purification of various proteins (Berna et al., 1997; Liu and Yu, 1990; Sulkowski, 1989). IMAC is also used to determine surface topography of proteins (Boden et al., 1998) and offers many advantages compared with chromatographic methods such as high binding capacity and high recovery yield, nondenaturing elution conditions beside cheapness and stability (Brena et al., 1994; Ordaz et al., 2000).…”

Section: Introductionmentioning

confidence: 99%

Poly-(l)-histidine immobilized cryogels for lysozyme purification

Çimen

Türkmen

Deni̇zli̇

2016

Adsorption Science & Technology

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Immobilized metal ion affinity chromatography is one of the methods used for the adsorption of proteins. In this study, poly(glycidyl methacrylate) cryogel discs were prepared by free radical polymerization. The metal chelating groups were polymeric chain of poly-(L)-histidine (mol wt ! 5000) having poly-imidazole ring sequence. Then, Cu(II), Zn(II), and Ni(II) ions were separately chelated on the poly-(L)-histidine immobilized poly(glycidyl methacrylate) cryogel discs to be used in immobilized metal ion affinity chromatography separation of lysozyme. The swelling test, Fourier transform infrared spectroscopy, Brunauer-Emmett-Teller, and scanning electron microscopy were performed to characterize both poly(glycidyl methacrylate) and poly-(L)-histidine immobilized poly(glycidyl methacrylate) cryogel discs. The effects of the pH, lysozyme concentration, adsorption time, and ionic strength on the adsorption capacity were studied. These parameters were varied between 4.0 and 8.0 for pH, 0.0 and 2.0 mg/ml for initial lysozyme concentration, 0 and 120 min for adsorption time, and 0.0 and 1.0 mM for ionic strength. The maximum lysozyme adsorption capacity of the Cu(II), Zn(II), and Ni(II) ions chelated poly-(L)-histidine immobilized poly(glycidyl methacrylate) cryogel discs was 36.4, 26.8, and 17.3 mg/g cryogel, respectively. Desorption of lysozyme from cryogel discs was easily achieved by 1.0 M NaCI solution. Repeated adsorption-elution processes showed that these cryogel discs were suitable for repeatable lysozyme adsorption. Adsorption isotherms fitted to Langmuir model and adsorption kinetics suited to pseudo-second order model. Thermodynamic parameters (i.e. DH , DS , DG) were also calculated from Langmuir isotherms at different temperatures.

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Section: Introductionmentioning

confidence: 99%

Poly-(l)-histidine immobilized cryogels for lysozyme purification

Çimen

Türkmen

Deni̇zli̇

2016

Adsorption Science & Technology

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“…When a protein mixture is percolated through an IMAC column, some proteins, which carry on their external surface amino acid residues with electron donor character, can bind to the chelated metal through the available coordination sites, and are hence adsorbed, while others elute from the column unretarded. On the basis of this principle, applications of IMAC range from the separation of small molecules such as amino acids (Fazakerley & Best, 1965), nucleotides (Hubert & Porath, 1981), or aromatic amines (Liu & Yu, 1990) to the purification of a variety of proteins (Sulkowski, 1985), including membrane glycoproteins (Corradini et al, 1988) and engineered proteins bearing synthetic metal affinity sites on their surface [for a review, see Arnold (1991)], and even further extend to the separation of intact cells (Botros & Vijayalaksmi, 1989). Moreover, the potential for high resolution of metal-based affinity purification has been previously demonstrated by the separation in a single chromatographic run of recombinant D-xylose isomerase from a crude cell lysate (Mrabet, 1992) or of 19 peptide hormones, some of which differ in their primary sequence only by the configuration (L or D) of a single amino acid (Nakagawa et al, 1988).…”

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confidence: 99%

Residue Accessibility, Hydrogen Bonding, and Molecular Recognition: Metal−Chelate Probing of Active Site Histidines in Chymotrypsins

et al. 1997

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Subspecies defining the maturation pathway of bovine chymotrypsinogen to alpha-chymotrypsin have been separated in a single chromatographic run by affinity to iminodiacetic acid-Cu(II) [IDA-Cu(II)] immobilized onto Novarose. A major highlight of the elution pattern is that, as maturation proceeds, these subspecies exhibit a correlated increase in affinity toward IDA-Cu(II). This behavior is analyzed by a combination of physicochemical and molecular modeling techniques to assess the contribution of the two histidines present in chymotrypsins, at positions 40 and 57 on the protein surface. Catalytic His-57 features adequate surface accessibility to serve as a ligand to IDA-Cu(II), but its participation is clearly ruled out by specific chemical modification. In contrast, His-40, whose side chain is buried in the crystal structures of both zymogen and mature enzyme, surprisingly proves the most plausible candidate as an electron donor to IDA-Cu(II). This apparent conflict between histidine accessibility and their implication in IDA-Cu(II) recognition has been rationalized on the basis of their flexibility and/or hydrogen-bonding status, with the following outcome. First, histidine constitutes a useful reporter group for subtle protein conformational fluctuations. Second, static accessibility computation alone provides no unequivocal guideline as to whether a protein residue can serve as a ligand. Third, this study is the first to document the occurrence of a screening effect due to hydrogen bonding of an otherwise "accessible" histidine. A significant corollary to this finding would be that the catalytic histidine is rigidly entrapped in a remarkably strong hydrogen-bonding network, a situation that may pertain to mechanistic aspects of catalysis.

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Epoxy-activated adsorbents in liquid chromatography of physiologically active substances (review)

Kuznetsov¹

1993

Pharm Chem J

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Copper(II)-iminodiacetic acid chelating resin as a stationary phase in the immobilized metal ion affinity chromatography of some aromatic amines

Cited by 7 publications

References 14 publications

Poly-(l)-histidine immobilized cryogels for lysozyme purification

Poly-(l)-histidine immobilized cryogels for lysozyme purification

Residue Accessibility, Hydrogen Bonding, and Molecular Recognition: Metal−Chelate Probing of Active Site Histidines in Chymotrypsins

Epoxy-activated adsorbents in liquid chromatography of physiologically active substances (review)

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