Immunofixation reveals an apparent α heavy chain caused by precipitation of fibrinogen with IgA antiserum

Jennifer A. Snyder, Monte Willis, David G. Grenache

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

Background: Fibrinogen present in serum specimens can interfere with the interpretation of serum protein electrophoresis. We report here the unexpected precipitation of fibrinogen by an IgA antiserum used in immunofixation electrophoresis. Methods: Immunofixation electrophoresis of plasma combined with ethanol precipitation, serial dilution of plasma, and fibrinogen adsorption of the antiserum were used to investigate the apparent immunoreactivity of a commercial source of IgA antiserum to fibrinogen. Results: Fibrinogen immunoreactivity by IgA antiserum was observed at fibrinogen concentrations ≥ 0.93 g/l. Ethanol precipitation of plasma removed fibrinogen and prevented the immunofixation of the protein by the IgA antiserum. Adsorption of the IgA antiserum with human fibrinogen removed its ability to precipitate fibrinogen, demonstrating cross-reactivity between the IgA antiserum and fibrinogen. Conclusions: Commercial sources of antiserum used for immunofixation electrophoresis may contain antibodies with specificity towards proteins typically absent from serum such as fibrinogen and can produce clinically misleading results.

Original languageEnglish (US)
Pages (from-to)192-194
Number of pages3
JournalClinica Chimica Acta
Volume368
Issue number1-2
DOIs
StatePublished - Jun 1 2006
Externally publishedYes

Fingerprint

Fibrinogen
Immunoglobulin A
Immune Sera
Electrophoresis
Plasmas
Adsorption
Ethanol
Antibody Specificity
Serum
Dilution
Blood Proteins
Precipitates
Proteins
Antibodies

Keywords

  • Fibrinogen
  • Heavy chain disease
  • Immunofixation electrophoresis
  • Interference
  • Serum protein electrophoresis

ASJC Scopus subject areas

  • Biochemistry
  • Clinical Biochemistry
  • Biochemistry, medical

Cite this

Immunofixation reveals an apparent α heavy chain caused by precipitation of fibrinogen with IgA antiserum. / Snyder, Jennifer A.; Willis, Monte; Grenache, David G.

In: Clinica Chimica Acta, Vol. 368, No. 1-2, 01.06.2006, p. 192-194.

Research output: Contribution to journalArticle

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abstract = "Background: Fibrinogen present in serum specimens can interfere with the interpretation of serum protein electrophoresis. We report here the unexpected precipitation of fibrinogen by an IgA antiserum used in immunofixation electrophoresis. Methods: Immunofixation electrophoresis of plasma combined with ethanol precipitation, serial dilution of plasma, and fibrinogen adsorption of the antiserum were used to investigate the apparent immunoreactivity of a commercial source of IgA antiserum to fibrinogen. Results: Fibrinogen immunoreactivity by IgA antiserum was observed at fibrinogen concentrations ≥ 0.93 g/l. Ethanol precipitation of plasma removed fibrinogen and prevented the immunofixation of the protein by the IgA antiserum. Adsorption of the IgA antiserum with human fibrinogen removed its ability to precipitate fibrinogen, demonstrating cross-reactivity between the IgA antiserum and fibrinogen. Conclusions: Commercial sources of antiserum used for immunofixation electrophoresis may contain antibodies with specificity towards proteins typically absent from serum such as fibrinogen and can produce clinically misleading results.",
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AU - Willis, Monte

AU - Grenache, David G.

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N2 - Background: Fibrinogen present in serum specimens can interfere with the interpretation of serum protein electrophoresis. We report here the unexpected precipitation of fibrinogen by an IgA antiserum used in immunofixation electrophoresis. Methods: Immunofixation electrophoresis of plasma combined with ethanol precipitation, serial dilution of plasma, and fibrinogen adsorption of the antiserum were used to investigate the apparent immunoreactivity of a commercial source of IgA antiserum to fibrinogen. Results: Fibrinogen immunoreactivity by IgA antiserum was observed at fibrinogen concentrations ≥ 0.93 g/l. Ethanol precipitation of plasma removed fibrinogen and prevented the immunofixation of the protein by the IgA antiserum. Adsorption of the IgA antiserum with human fibrinogen removed its ability to precipitate fibrinogen, demonstrating cross-reactivity between the IgA antiserum and fibrinogen. Conclusions: Commercial sources of antiserum used for immunofixation electrophoresis may contain antibodies with specificity towards proteins typically absent from serum such as fibrinogen and can produce clinically misleading results.

AB - Background: Fibrinogen present in serum specimens can interfere with the interpretation of serum protein electrophoresis. We report here the unexpected precipitation of fibrinogen by an IgA antiserum used in immunofixation electrophoresis. Methods: Immunofixation electrophoresis of plasma combined with ethanol precipitation, serial dilution of plasma, and fibrinogen adsorption of the antiserum were used to investigate the apparent immunoreactivity of a commercial source of IgA antiserum to fibrinogen. Results: Fibrinogen immunoreactivity by IgA antiserum was observed at fibrinogen concentrations ≥ 0.93 g/l. Ethanol precipitation of plasma removed fibrinogen and prevented the immunofixation of the protein by the IgA antiserum. Adsorption of the IgA antiserum with human fibrinogen removed its ability to precipitate fibrinogen, demonstrating cross-reactivity between the IgA antiserum and fibrinogen. Conclusions: Commercial sources of antiserum used for immunofixation electrophoresis may contain antibodies with specificity towards proteins typically absent from serum such as fibrinogen and can produce clinically misleading results.

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