An enzyme immunoassay for the detection of staphylococcal protein A in affinity-purified products

Dertzbaugh, Mark T.; Flickinger, Michael C.; Lebherz, William B.

doi:10.1016/0022-1759(85)90070-5

Cited by 19 publications

(4 citation statements)

References 8 publications

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“…A number of studies have demonstrated that antibody preparations purified using Protein A affinity chromatographic method are inevitably contaminated with Protein A to differing extent depending on the chemistry used in linking Protein A to the solid support (Dertzbaugh et al 1985;Duffy et al 1989;Fuglistaller 1989;Godfry et al 1992Godfry et al , 1993Huse et al 2002). The injection of antibodies contaminated with Protein A into people can induce dangerous immunological responses in the host (Ainsworth et al 1990).…”

Section: Peptidyl Protein a Mimetic Affinity Ligandsmentioning

confidence: 96%

“…The concentration of antibody in the test solution would have "swarmed" the I 125 -Protein A, rendering the test invalid. Dertzbaugh et al (1985) developed an enzyme immunoassay for detecting Protein A in affinity purified antibody products using alkaline phosphatase labeled anti-Protein A antibody conjugates and a solid phase anti-Protein A. The use of two antibodies specific to Protein A makes it possible to measure the presence of Protein A in the immunoglobulin fractions.…”

Section: Macromolecular Affinity Ligandsmentioning

confidence: 99%

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Affinity Chromatographic Purification of Antibodies

2007

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Affinity chromatographic methods for purifying antibodies are reviewed. Topics reviewed include (a) the matrices used in the preparation of the affinity supports; (b) the chemistries commonly used to attach affinity ligands directly on hydroxyl-carrying supports and indirectly through the use of bifunctional agents to crosslink the affinity ligands to the supports; (c) methods for detecting ligand leakage; (d) macromolecular affinity ligands; (e) low molecular weight peptidyl affinity ligands; (f) low molecular weight non-peptidyl affinity ligands; (g) optimal conditions for achieving improved product yield; and (h) optimal elution systems that minimize the denaturation of the purified antibodies.

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Section: Peptidyl Protein a Mimetic Affinity Ligandsmentioning

confidence: 96%

Section: Macromolecular Affinity Ligandsmentioning

confidence: 99%

Affinity Chromatographic Purification of Antibodies

2007

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“…16 This effect may be reduced by the inclusion of nucleophilic compounds such as glycine in the adsorption and washing buffers, although their presence may also result in an increase in background Ab leakage from agarose preparations. 17 Ubrich and co-workers 18 compared the stability of immunosorbents prepared by a number of immobilisation chemistries. From their findings, the five coupling chemistries referred to in Table 2 could be ranked from best to worst, on the basis of the amount of Ab bound, as DVS > TC > CNBr > CDI > epoxide.…”

Section: Matrix Activationmentioning

confidence: 99%

Immunoaffinity extraction in veterinary residue analysis—a regulatory viewpoint†‡

Godfrey¹

1998

Analyst

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The utility of immunoaffinity chromatography (IAC) for the purification of veterinary drug residues from extracts of foods of animal origin is widely acknowledged. However owing to the unique nature of the specific antibody reagent used when synthesising an immunosorbent, certain reassurances are needed before an IAC process can be considered an acceptable stage in a routine analytical method. European Community legislation requires applicants for Maximum Residue Limits or national Marketing Authorization for veterinary medicinal products, used in food producing animals, to provide a routine analytical method in accordance with Volume VI of the Rules Governing Medicinal Products in the European Community. In order to ensure the continued supply of immunosorbent material, applicants wishing to use IAC sample clean-up procedures should consider generating the following data: a standard operating procedure (SOP) for antibody production (or cell-line maintenance in the case of monoclonal antibodies), a specifications document of antibody characterisation, an SOP for immunosorbent synthesis, validation of immunosorbent operating conditions and an assessment of its performance criteria. This paper aims to introduce analysts to the technique of IAC and to suggest how those areas of concern highlighted above may be addressed.

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“…Also the potential leakage from the matrix or proteolytic degradation of protein-based affinity ligands for IgG may contaminate the eluted IgG. Such contaminations can create severe allergic response in some patients (Dertzbaugh et al 1985;Bloom et al 1989;Fuglistaller 1989).…”

Section: Introductionmentioning

confidence: 98%

In‐Tandem Column Arrangement for Rapid Purification of IgG using a Blue Avid Gel P and an Aza‐Arenophilic Affinity Gel

2007

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An in-tandem study comprising two affinity chromatographic columns, Blue Avidgel P (for the selective removal of albumin) and an aza-arenophilic gel (Gel A) containing a nitrogen capping nucleophile (for the selective removal of IgG), was conducted to obtain high purity IgG from serum. The results demonstrated that highly pure IgG (.97%) can be obtained from the phenethylamine capped aza-arenophilic gel column after the serum was passed through the Blue Avidgel P column in contrast to the 38% IgG purity obtained when the serum was passed through a Gel A column alone under similar conditions. Further studies show that IgG selectivity is not dependent on the nature of the support material used in the synthesis of these aza-arenophilic gels since the synthesis of aza-arenophilic gels using either Sepharose or Fractogel yield similar results.

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An enzyme immunoassay for the detection of staphylococcal protein A in affinity-purified products

Cited by 19 publications

References 8 publications

Affinity Chromatographic Purification of Antibodies

Affinity Chromatographic Purification of Antibodies

Immunoaffinity extraction in veterinary residue analysis—a regulatory viewpoint†‡

In‐Tandem Column Arrangement for Rapid Purification of IgG using a Blue Avid Gel P and an Aza‐Arenophilic Affinity Gel

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