%0 Journal Article %1 citeulike:477528 %A Corsini, A. %A Fantappiè, S. %A Marcovina, S. %A Granata, A. %A Fumagalli, R. %A Catapano, A. L. %C Institute of Pharmacological Sciences, University of Milan, Italy. %D 1989 %J Biochem Biophys Res Commun %K mapping epitope apob %N 3 %P 908--915 %T Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2475112 %V 162 %X In a panel of 10 monoclonal antibodies raised against human LDL we detected three antibodies (named 5A, 6B, and 6E) which recognize both apolipoprotein B-100 and B-48. Antibody 5A inhibited, in a dose dependent manner, the interaction of 125I-LDL with their receptor on human skin fibroblasts. Using thrombolytic fragments, the epitope of antibody 5A was mapped to the carboxy terminal region of apo B-48. MAB 5A was equipotent with MAB Mb 47, an inhibitory antibody whose epitope lies near a putative receptor binding domain of apo B in thrombolytic fragment T2. These findings suggest that areas other than the carboxy terminal portion of apo B-100 may participate in the LDL-receptor interaction, either directly or by determining the exposition of high affinity sites of apo B-100.

@article{citeulike:477528, abstract = {In a panel of 10 monoclonal antibodies raised against human LDL we detected three antibodies (named 5A, 6B, and 6E) which recognize both apolipoprotein B-100 and B-48. Antibody 5A inhibited, in a dose dependent manner, the interaction of 125I-LDL with their receptor on human skin fibroblasts. Using thrombolytic fragments, the epitope of antibody 5A was mapped to the carboxy terminal region of apo B-48. MAB 5A was equipotent with MAB Mb 47, an inhibitory antibody whose epitope lies near a putative receptor binding domain of apo B in thrombolytic fragment T2. These findings suggest that areas other than the carboxy terminal portion of apo B-100 may participate in the LDL-receptor interaction, either directly or by determining the exposition of high affinity sites of apo B-100.}, added-at = {2006-07-07T01:10:50.000+0200}, address = {Institute of Pharmacological Sciences, University of Milan, Italy.}, author = {Corsini, A. and Fantappiè, S. and Marcovina, S. and Granata, A. and Fumagalli, R. and Catapano, A. L.}, biburl = {https://www.bibsonomy.org/bibtex/28a5794e6f329c353fcea2f5897cbd46b/biblio24}, citeulike-article-id = {477528}, interhash = {3029ee1343e4f8a5d28aee59f4c5c89e}, intrahash = {8a5794e6f329c353fcea2f5897cbd46b}, issn = {0006-291X}, journal = {Biochem Biophys Res Commun}, keywords = {mapping epitope apob}, month = {August}, number = 3, pages = {908--915}, priority = {2}, timestamp = {2006-07-07T01:10:50.000+0200}, title = {Monoclonal antibody 5A binds apolipoprotein B-48 and inhibits the low density lipoprotein-receptor interaction.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=2475112}, volume = 162, year = 1989 }