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Patwardhan, Anshuman V.; Goud, Gaddam Narsa; Pasquinelli, Richard S.; Koepsel, Richard R.; Ataai, Mohammad M.

doi:10.1023/a:1008842902587

Cited by 19 publications

(17 citation statements)

References 8 publications

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“…This active region does not coincide with the active center of the enzyme and the role of histidine residues is to form coordinating complexes with copper and zinc ions. Patwardhan et al [39] are of the opinion that peptides with two histidine residues have higher affinity toward copper ions than peptides with more histidine residues due to their lower sensitivity to pH changes. According to reference data, the high affinity of peptides with only one histidine residue can be explained by the presence of hydrophobic residues in close proximity to this amino acid.…”

Section: Resultsmentioning

confidence: 99%

Anti-Free-Radical Properties of the Peptide Fractions Isolated from String Bean by Immobilized Metal Ion Affinity Chromatography

Karaś¹

2007

PPL

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In this study, peptides and proteins extracted from string bean with 1% TCA were separated by chromatography on columns with copper ions immobilized through IDA and o-phosphoserine OPS. Protein and peptide concentrations and the anti-free-radical properties of the isolated fractions were determined. Identification was obtained using mass spectrometry. The anti-free- radical activity of all analyzed samples was determined using the DPPH test, and was found to depend on reaction time, choice of chelating agent and the order in which the fractions were eluted from the column.

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Section: Resultsmentioning

confidence: 99%

Anti-Free-Radical Properties of the Peptide Fractions Isolated from String Bean by Immobilized Metal Ion Affinity Chromatography

Karaś¹

2007

PPL

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“…In addition, factors such as the accessibility, microenvironment of the binding residue, co-operation between neighboring amino acid side chains, and local conformations play important roles in biomolecule adsorption. 16 Tryptophan also has some contributions. 17 The low cost of metals and the ease of regeneration of the supports are the attractive features of metal affinity separation.…”

Section: Introductionmentioning

confidence: 99%

Antibody purification from human plasma by metal‐chelated affinity membranes

Yavuz

Bereli

Armutçu

et al. 2011

J of Applied Polymer Sci

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The aim of this study is to investigate in detail the feasibility of poly(2-hydroxyethyl methacrylate-N-methacryloyl-(L)-histidine methyl ester), PHEMAH membranes for purification of immunoglobulin G (IgG) from human plasma. PHEMAH membranes were prepared by photo-polymerization technique. Then, Zn 2þ , Ni 2þ , Co 2þ , and Cu 2þ ions were chelated directly on the PHEMAH membranes. Elemental analysis assay was performed to determine the nitrogen content and polymerized MAH was calculated as 168.5 lmol/g. The nonspecific IgG adsorption onto the plain PHEMA membranes was negligible (about 0.25 mg/mL). A remarkable increase in the IgG adsorption capacities were achieved from human plasma with PHEMAH membranes (up to 68.4 mg/mL).Further increase was observed with the metal-chelated PHEMAH membranes (up to 118 mg/mL). The metal-chelate affinity membranes allowed the one-step separation of IgG from human plasma. The binding range of metal ions for surface histidines from human plasma followed the order: Cu 2þ > Ni 2þ > Zn 2þ > Co 2þ . Adsorbed IgG was eluted using 250 mM EDTA with a purity of 94.1%. IgG molecules could be repeatedly adsorbed and eluted with the metal-chelated PHEMAH membranes without noticeable loss in their IgG adsorption capacity.

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“…The other factors contributing to bimolecular adsorption are aromatic amino acids and amino terminus of the peptides, microenvironment of the binding residue, co-operation between neighbouring amino acid side chains and local conformations [23]. The fascinating features of metal affinity separation are low cost of metals and the ease of regeneration of the support [24,25].…”

Section: Introductionmentioning

confidence: 99%