Histidine ligand affinity chromatography

Vijayalakshmi, M.A.

doi:10.1007/bf02761713

Cited by 28 publications

(6 citation statements)

References 17 publications

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“…The histidine-agarose support used in this work presents this type of structure, with histidine ligands located at the terminus of long hydrophobic arms grafted on the beads. The capacity of histidinebased supports for several proteins has been studied by Vijayalakshmi (1996). For a histidine support with a ligand density of 10 µmol his/mL gel, the capacities obtained were a function of the protein being studied, varying between 0.5 and 1.0 mg protein/mL gel.…”

Section: Resultsmentioning

confidence: 99%

Dynamic binding capacity of plasmid DNA in histidine–agarose chromatography

Sousa

Prazeres

Queiroz

2007

Biomedical Chromatography

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The use of histidine-agarose chromatography in the purification of supercoiled (sc) plasmid DNA (pDNA) from Escherichia coli lysates has been reported recently. In the current work we describe a set of breakthrough experiments which were designed to study the effect of parameters such as flow-rate, temperature, concentration and conformation on the dynamic binding capacity of pDNA to the histidine support. One of the most striking results shows that the dynamic binding capacity for sc pDNA decreases linearly from 250.8 to 192.0 microg sc pDNA/mL when the temperature is varied from 5 to 24 degrees C. This behaviour was attributed to temperature-induced, pre-denaturation conformational changes which promote the removal of negative superhelical turns in sc pDNA molecules and decrease the interaction of DNA bases with the histidine ligands. The capacity for sc pDNA was highly improved when using feeds with higher pDNA concentrations, a phenomenon which was attributed to the fact that pDNA molecules in more concentrated solutions are significantly compressed. A maximum capacity of 530.0 microg pDNA/mL gel was obtained when using a 125 microg/mL pDNA feed at 1 mL/min and 5 degrees C, a figure which is comparable to the plasmid capacity values published for other chromatographic supports. Finally, a more than 2-fold increase in capacity was obtained when changing from open circular to sc pDNA solutions. Overall, the results obtained provide valuable information for the future development and implementation of histidine chromatography in the process scale purification of pDNA.

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Section: Resultsmentioning

confidence: 99%

Dynamic binding capacity of plasmid DNA in histidine–agarose chromatography

Sousa

Prazeres

Queiroz

2007

Biomedical Chromatography

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“…Histidine has been previously identified as a ligand for IgG (26–34). Histidine was coupled on Sepharose or silica particles through its carboxyl group (27–29) or immobilized via its amino group on poly(ethylene vinyl alcohol) hollow‐fiber membrane (30–32) or on poly(2‐hydroxyethylmethacrylate) beads (34).…”

Section: Resultsmentioning

confidence: 99%

Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G

Yang

Gurgel

Carbonell

2005

The Journal of Peptide Research

123

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A family of linear hexapeptides composed of histidine on the N‐terminus followed by aromatic amino acid(s) and positively charged amino acid(s) has been identified through a three‐step screening of a synthetic solid phase library. These peptides were able to recognize human immunoglobulin G (HIgG) through its Fc region, and their selectivity to Fc is comparable to Protein A. This is the first known report of short peptides that are able to bind HIgG by recognizing its Fc portion. One of the ligands from the identified family, HWRGWV, was examined for its ability to isolate HIgG from complex mixtures. It was found that HWRGWV possessed the potential to purify HIgG from complete mammalian cell culture medium containing 10% fetal calf serum with purity comparable to commercially available resins, but using milder elution conditions. HWRGWV bound all HIgG subclasses and IgGs from bovine, mouse, goat, and rabbit. The broad affinity spectrum as well as its Fc recognition ability may be useful in capturing and detecting both polyclonal and monoclonal antibodies.

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“…Histidine ligands have subsequently proved to be useful for enrichment and purification of many other proteins. 402 Subtractive affinity chromatography on immobilized antihuman albumin and antihuman transferrin IgGs was described by Wheatley 403 techniques have also been used to monitor the production of antibodies in hybridoma cultures, by using nonporous silica columns with immobilized Fc receptors. 404 …”

Section: Bioaffinity Chromatographymentioning

confidence: 99%

High‐Performance Liquid Chromatography of Biological Macromolecules

Irgum¹

2000

Encyclopedia of Analytical Chemistry

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Histidine ligand affinity chromatography

Cited by 28 publications

References 17 publications

Dynamic binding capacity of plasmid DNA in histidine–agarose chromatography

Dynamic binding capacity of plasmid DNA in histidine–agarose chromatography

Hexamer peptide affinity resins that bind the Fc region of human immunoglobulin G

High‐Performance Liquid Chromatography of Biological Macromolecules

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