%0 Journal Article %1 citeulike:503600 %A Koren, E. %A Solter, D. %A Lee, D. M. %A Reiner, Z. %A McConathy, W. J. %A Dashti, N. %A Alaupovic, P. %D 1986 %J Biochim Biophys Acta %K affinity antibody apob %N 1 %P 91--100 %T Characterization of a monoclonal antibody that binds equally to all apolipoprotein and lipoprotein forms of human plasma apolipoprotein B. I. Specificity and binding studies. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=3081046 %V 876 %X A stable mouse hybridoma cell line has been developed that produces monoclonal antibody to human plasma apolipoprotein B. This antibody was proven to be specific for apolipoprotein B immunoblotting and an enzyme immunoassay using apolipoprotein B and other apolipoproteins. The antibody bound with comparable affinities to soluble apolipoprotein B, chylomicrons, very-low-density (VLDL) and low-density lipoproteins (LDL). Coupled to agarose, this antibody allowed complete removal of apolipoprotein B-containing lipoproteins from normolipidemic, hypertriglyceridemic and hypercholesterolemic plasma. Desialyzation and deglycosylation had no effect on its binding to LDL. The described antibody had no effect on the receptor-mediated binding of radiolabeled LDL to the human hepatoma cells (HepG2) in culture. Analysis of 25 different samples of human plasma indicated identical expression of the corresponding epitope in these individuals. The described monoclonal antibody, most likely, binds to a rather stable domain of apolipoprotein B that is not altered by the interaction with lipids or polymorphism of the apolipoprotein B. We propose that this antibody be called 'Pan B' antibody.

@article{citeulike:503600, abstract = {A stable mouse hybridoma cell line has been developed that produces monoclonal antibody to human plasma apolipoprotein B. This antibody was proven to be specific for apolipoprotein B immunoblotting and an enzyme immunoassay using apolipoprotein B and other apolipoproteins. The antibody bound with comparable affinities to soluble apolipoprotein B, chylomicrons, very-low-density (VLDL) and low-density lipoproteins (LDL). Coupled to agarose, this antibody allowed complete removal of apolipoprotein B-containing lipoproteins from normolipidemic, hypertriglyceridemic and hypercholesterolemic plasma. Desialyzation and deglycosylation had no effect on its binding to LDL. The described antibody had no effect on the receptor-mediated binding of radiolabeled LDL to the human hepatoma cells (HepG2) in culture. Analysis of 25 different samples of human plasma indicated identical expression of the corresponding epitope in these individuals. The described monoclonal antibody, most likely, binds to a rather stable domain of apolipoprotein B that is not altered by the interaction with lipids or polymorphism of the apolipoprotein B. We propose that this antibody be called 'Pan B' antibody.}, added-at = {2006-07-07T01:10:50.000+0200}, author = {Koren, E. and Solter, D. and Lee, D. M. and Reiner, Z. and McConathy, W. J. and Dashti, N. and Alaupovic, P.}, biburl = {https://www.bibsonomy.org/bibtex/224b7357b404b478a9f4b77478dfbb9ce/biblio24}, citeulike-article-id = {503600}, interhash = {0e058233d974197de8e59b5186e6d6e6}, intrahash = {24b7357b404b478a9f4b77478dfbb9ce}, issn = {0006-3002}, journal = {Biochim Biophys Acta}, keywords = {affinity antibody apob}, month = {March}, number = 1, pages = {91--100}, priority = {2}, timestamp = {2006-07-07T01:10:50.000+0200}, title = {Characterization of a monoclonal antibody that binds equally to all apolipoprotein and lipoprotein forms of human plasma apolipoprotein B. I. Specificity and binding studies.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=3081046}, volume = 876, year = 1986 }