Clinical Chemistry
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Clinical Chemistry 24: 455-459, 1978;
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Clinical Chemistry, Vol 24, 455-459, Copyright © 1978 by American Association for Clinical Chemistry

Enzyme immunoassay for human apolipoprotein B, the major protein moiety in low-density- and very-low-density lipoproteins

JC Fruchart, C Desreumaux, P Dewailly, G Sezille, J Jaillard, Y Carlier, D Bout and A Capron

We used enzyme immunoassay to measure apolipoprotein B concentration in human plasma. Pure lipoprotein B was isolated from serum samples of fasting normolipidemic subjects by sequential preparative ultracentrifugation and coated to a polystyrene tube surface by adsorption. Human serum samples and rabbit antiserum to human apolipoprotein B were incubated with the solid-phase lipoprotein B. Soluble antigen competed with solid-phase antigen for binding to antibodies. After washing, peroxidase-labeled sheep antibodies against rabbit immunoglobulins were added, and after further washing the bound label was assayed. This provided a direct measurement of the soluble antigen. The best technical conditions for the assay were determined. The minimum detectable concentration was 1 microgram per assay. The enzyme immunoassay yielded values that compare favorably with those obtained by radial immunodiffusion (r = 0.84) and by rocket immunoelectrophoresis (r = 0.80). The assay offers several advantages over existing techniques: sensitivity, specificity, simplicity, ane non- use of radioisotopes.




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Copyright © 1978 by the American Association for Clinical Chemistry.