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Related Experiment Videos

Standardization for four protein analytes with the Behring Nephelometer.

S B Schotters1, J H McBride, D O Rodgerson

  • 1Department of Pathology, UCLA School of Medicine 90024.

Clinical Chemistry
|September 1, 1988
PubMed
Summary

Commercial protein calibrators showed higher immunoglobulin G, A, and M values on the Behring Nephelometer. Standardization with WHO and RPSP II preparations proved unsuitable for accurate protein quantification.

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Area of Science:

  • Clinical Chemistry
  • Immunology
  • Biochemistry

Background:

  • Initial immunoglobulin G (IgG), A, and M assays using the Behring Nephelometer yielded higher than expected values.
  • Verification of commercial protein calibrators was necessary to address these discrepancies.

Purpose of the Study:

  • To verify the accuracy of commercial protein calibrators for immunoglobulin and transferrin quantification.
  • To assess the suitability of World Health Organization (WHO) and Reference Preparation for Serum Proteins II (RPSP II) as standardization materials.

Main Methods:

  • Standardization of the Behring Nephelometer using WHO International Reference Preparation for Human Serum Immunoglobulins G, A, and M.
  • Standardization using the RPSP II for immunoglobulins and transferrin.

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  • Preparation and analysis of primary standards from individual purified proteins (IgG, IgA, IgM, transferrin).

    • Main Results:

    • Analytical recoveries of commercial calibrators varied significantly.
    • WHO and RPSP II preparations were deemed unsuitable as benchmark calibrators due to assigned protein concentrations.
    • Successful standardization was achieved for transferrin and IgG primary standards.
    • IgA and IgM primary standards exhibited less than 100% antigenicity, necessitating adjustments or removal of nonreactive components.

    Conclusions:

    • Existing commercial protein calibrators and international reference materials are not ideal for standardizing the Behring Nephelometer for all targeted proteins.
    • Further research is required to identify suitable purified materials for accurate IgA and IgM standardization.