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Clinical chemistry1979; 25(10); 1749-1756;

Identification of alpha1-lipoproteins in crossed immunoelectrophoresis.

Abstract: Evans Blue dye binds selectively, but with different avidities, to five major antigens in human serum. The anodic mobility of the antigen-dye complexes is greater than that of the antigens alone in crossed immunoelectrophoresis, which is of practical value for identification. We used this characteristic to show that in some human sera there is a population of alpha1-lipoprotein molecules that migrates electrophoretically in the beta-lipoprotein region, where in conventional zone electrophoresis it could be mistaken for beta-lipoprotein. We also demonstrate that horses, unlike rabbits, rarely make precipitins to human serum alpha1-lipoprotein. Equine antiserum to human serum therefore generally is useless for detecting this important serum antigen in immunoelectrophoresis.
Publication Date: 1979-10-01 PubMed ID: 225059
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  • Journal Article

Summary

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This research investigated the identification of a specific type of protein, alpha1-lipoprotein, in human serum samples using a method called crossed immunoelectrophoresis. The scientists found that it is possible for these proteins to behave in a way that could lead to mistaken identification during testing. The study also revealed that horse antiserum generally fails to reveal these proteins, unlike rabbit antiserum.

Understanding Proteins in the Study

  • The research primarily focused on a type of proteins known as alpha1-lipoproteins in human serum (blood liquid). Proteins carry out most of the biological functions and are critical for the structure, function, and regulation of body tissues and organs.
  • The study highlights the issue of potential misinterpretation while identifying the alpha1-lipoprotein owing to its tendency to migrate, or move, into the area typically associated with beta-lipoproteins during a test known as zone electrophoresis.

Technique Used: Crossed Immunoelectrophoresis

  • Crossed immunoelectrophoresis is a lab technique used to separate and identify proteins. In this study, it’s used to distinguish the alpha1-lipoproteins.
  • A characteristic property that Evans Blue dye binds to certain proteins with varying degrees of strength is harnessed for identification in this method.
  • Interestingly, the dye-protein complexes demonstrate a higher rate of movement towards the anode (+ve terminal) compared with the proteins alone, a feature found beneficial for identification purposes.

Comparing Different Antisera

  • The experiment revealed a substantial difference between horse antiserum and rabbit antiserum’s response to human serum alpha1-lipoprotein. Horse antiserum, unlike rabbit antiserum, rarely produces precipitins (proteins that react with specific antigens) to human serum alpha1-lipoproteins.
  • As a result, horse antiserum is generally ineffective for detecting this significant serum antigen in immunoelectrophoresis.

Implications of the Research

  • This research provides valuable insights and warning of possible misinterpretation while identifying specific proteins in human serum.
  • It further brings to light the importance of properly selecting the antiserum type based on the nature of the study, given the significant difference in their effectiveness in detecting certain proteins.

Cite This Article

APA
Cline LJ, Crowle AJ. (1979). Identification of alpha1-lipoproteins in crossed immunoelectrophoresis. Clin Chem, 25(10), 1749-1756.

Publication

ISSN: 0009-9147
NlmUniqueID: 9421549
Country: England
Language: English
Volume: 25
Issue: 10
Pages: 1749-1756

Researcher Affiliations

Cline, L J
    Crowle, A J

      MeSH Terms

      • Evans Blue
      • Humans
      • Immunoelectrophoresis, Two-Dimensional / methods
      • Lipoproteins, HDL / blood
      • Transferrin

      Citations

      This article has been cited 2 times.
      1. Emmett M, Crowle AJ. Crossed immunoelectrophoresis: qualitative and quantitative considerations. J Immunol Methods 1982;50(2):R65-83.
        doi: 10.1016/0022-1759(82)90218-6pubmed: 7045231google scholar: lookup
      2. Emmett M, Cerniglia CE, Crowle AJ. Differential serum protein binding of benzidine- and benzidine-congener based dyes and their derivatives. Arch Toxicol 1985 Jun;57(2):130-5.
        doi: 10.1007/BF00343123pubmed: 4026572google scholar: lookup