%0 Journal Article %1 citeulike:477512 %A Gries, A. %A Fievet, C. %A Marcovina, S. %A Nimpf, J. %A Wurm, H. %A Mezdour, H. %A Fruchart, J. C. %A Kostner, G. M. %C Institute of Physiology, University of Graz, Austria. %D 1988 %J J Lipid Res %K mapping epitope apob %N 1 %P 1--8 %T Interaction of LDL, Lpa, and reduced Lpa with monoclonal antibodies against apoB. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2451704 %V 29 %X 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), lipoproteina (Lpa), and reduced Lpa. 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 apolipoproteina. 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, Lpa, and reduced Lpa. Antibodies 2A and 6B bound about twofold better to LDL and reduced Lpa than to untreated Lpa. Antibodies L3 and L7 needed nearly threefold higher amounts of Lpa-apoB for 50% inhibition of antibody binding than of apoB of LDL and reduced Lpa. The amount of apoB required for 50% inhibition of antibody binding was somewhat higher in inhibitive assay than in competitive assay. We suggest that apoa covers certain epitopes of apoB in native Lpa leading to a reduced reaction with the monoclonal antibodies. However, it could also be that the binding of the aantigen to apoB via disulfide bridges causes profound conformational changes of the apoB region exposed to the surface.

@article{citeulike:477512, 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.}, added-at = {2006-07-07T01:10:50.000+0200}, address = {Institute of Physiology, University of Graz, Austria.}, author = {Gries, A. and Fievet, C. and Marcovina, S. and Nimpf, J. and Wurm, H. and Mezdour, H. and Fruchart, J. C. and Kostner, G. M.}, biburl = {https://www.bibsonomy.org/bibtex/2c2f02dd34a1c927e4d1496d639f195f1/biblio24}, citeulike-article-id = {477512}, interhash = {d178b51f5511a8a8e55cebe8a1e1fc96}, intrahash = {c2f02dd34a1c927e4d1496d639f195f1}, issn = {0022-2275}, journal = {J Lipid Res}, keywords = {mapping epitope apob}, month = {January}, number = 1, pages = {1--8}, priority = {2}, timestamp = {2006-07-07T01:10:50.000+0200}, title = {Interaction of LDL, Lp[a], and reduced Lp[a] with monoclonal antibodies against apoB.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=2451704}, volume = 29, year = 1988 }