Gewählte Publikation:
Gries, A; Fievet, C; Marcovina, S; Nimpf, J; Wurm, H; Mezdour, H; Fruchart, JC; Kostner, GM.
Interaction of LDL, Lpa, and reduced Lpa with monoclonal antibodies against apoB.
J Lipid Res. 1988; 29(1):1-8
Doi: 10.1016/S0022-2275(20)38555-2
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- Führende Autor*innen der Med Uni Graz
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Gries Anna
- Co-Autor*innen der Med Uni Graz
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Kostner Gerhard
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- Abstract:
- Five monoclonal antibodies (2A, 9A, 6B, L3, L7) produced in mice against human apolipoprotein B were investigated by competitive and inhibitive electroimmunoassay (EIA) for their reactivity with low density lipoprotein (LDL), lipoprotein[a] (Lp[a]), and reduced Lp[a]. All of the antibodies reacted with apoB of the different lipoproteins indicated by very similar slopes of the binding curves. None of them gave a positive reaction with apolipoprotein[a]. The amount of apoB required for 50% inhibition of antibody binding varied for the different antibodies and lipoproteins. Antibody 9A showed almost the same affinity for LDL, Lp[a], and reduced Lp[a]. Antibodies 2A and 6B bound about twofold better to LDL and reduced Lp[a] than to untreated Lp[a]. Antibodies L3 and L7 needed nearly threefold higher amounts of Lp[a]-apoB for 50% inhibition of antibody binding than of apoB of LDL and reduced Lp[a]. The amount of apoB required for 50% inhibition of antibody binding was somewhat higher in inhibitive assay than in competitive assay. We suggest that apo[a] covers certain epitopes of apoB in native Lp[a] leading to a reduced reaction with the monoclonal antibodies. However, it could also be that the binding of the [a]antigen to apoB via disulfide bridges causes profound conformational changes of the apoB region exposed to the surface.
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Antibodies, Monoclonal - immunology
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Apolipoproteins B - immunology
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Epitopes - immunology
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Humans - immunology
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Immunoelectrophoresis - immunology
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Lipoprotein(a) - immunology
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Lipoproteins - analysis
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