A monoclonal antibody (MB-19) was used to investigate the polymorphism of apolipoprotein B in a large family and in unrelated subjects. Apolipoprotein B was shown to exhibit high-, intermediate- or low-affinity binding to this antibody. Thus, MB-19 bound strongly to the Ag(c) epitope, An Ag antigenic domain previously characterized by human antisera, while it bound only weakly to the allelic epitope Ag(g). It proved therefore useful for the detection of the two corresponding allelic apoB species designated apoBc (high-affinity binding) and apoBg (low-affinity binding), and for confirming their co-dominant transmission. Intermediate binding resulted from the presence of a mixture of both apoB populations in heterozygous subjects.
%0 Journal Article
%1 citeulike:612402
%A Tikkanen, M. J.
%A Ehnholm, C.
%A Bütler, R.
%A Young, S. G.
%A Curtiss, L. K.
%A Witztum, J. L.
%D 1986
%J FEBS Lett
%K mapping polymorphism epitope antibody apob
%N 1
%P 54--58
%R 10.1016/0014-5793(86)80648-2
%T Monoclonal antibody detects Ag polymorphism of apolipoprotein B.
%U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=2424787
%V 202
%X A monoclonal antibody (MB-19) was used to investigate the polymorphism of apolipoprotein B in a large family and in unrelated subjects. Apolipoprotein B was shown to exhibit high-, intermediate- or low-affinity binding to this antibody. Thus, MB-19 bound strongly to the Ag(c) epitope, An Ag antigenic domain previously characterized by human antisera, while it bound only weakly to the allelic epitope Ag(g). It proved therefore useful for the detection of the two corresponding allelic apoB species designated apoBc (high-affinity binding) and apoBg (low-affinity binding), and for confirming their co-dominant transmission. Intermediate binding resulted from the presence of a mixture of both apoB populations in heterozygous subjects.
@article{citeulike:612402,
abstract = {A monoclonal antibody (MB-19) was used to investigate the polymorphism of apolipoprotein B in a large family and in unrelated subjects. Apolipoprotein B was shown to exhibit high-, intermediate- or low-affinity binding to this antibody. Thus, MB-19 bound strongly to the Ag(c) epitope, An Ag antigenic domain previously characterized by human antisera, while it bound only weakly to the allelic epitope Ag(g). It proved therefore useful for the detection of the two corresponding allelic apoB species designated apoBc (high-affinity binding) and apoBg (low-affinity binding), and for confirming their co-dominant transmission. Intermediate binding resulted from the presence of a mixture of both apoB populations in heterozygous subjects.},
added-at = {2006-07-07T01:10:50.000+0200},
author = {Tikkanen, M. J. and Ehnholm, C. and Bütler, R. and Young, S. G. and Curtiss, L. K. and Witztum, J. L.},
biburl = {https://www.bibsonomy.org/bibtex/218cacbf727f6c638aae0ffcd5744d016/biblio24},
citeulike-article-id = {612402},
doi = {10.1016/0014-5793(86)80648-2},
interhash = {2c5c26e4388d861fd9da93246cc35400},
intrahash = {18cacbf727f6c638aae0ffcd5744d016},
issn = {0014-5793},
journal = {FEBS Lett},
keywords = {mapping polymorphism epitope antibody apob},
month = {June},
number = 1,
pages = {54--58},
priority = {2},
timestamp = {2006-07-07T01:10:50.000+0200},
title = {Monoclonal antibody detects Ag polymorphism of apolipoprotein B.},
url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=2424787},
volume = 202,
year = 1986
}