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Generation of region‐specific antibodies to modified proteins
Author(s) -
Curtiss Linda K.,
Steinbrecher Urs P.,
Witztum Joseph L.
Publication year - 1987
Publication title -
journal of clinical laboratory analysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.536
H-Index - 50
eISSN - 1098-2825
pISSN - 0887-8013
DOI - 10.1002/jcla.1860010304
Subject(s) - lysine , acetylation , chemistry , antibody , monoclonal antibody , biochemistry , epitope , posttranslational modification , uremia , amino acid , immunology , medicine , gene , enzyme
Nonenzymatic modifications of the ϵ‐ amine of lysine residues in proteins have been described in diabetes, uremia, high‐dose aspirin therapy, and alcoholism. In this review, we describe the generation of lysine‐modification‐specific antibodies that can be used to identify and to quantitate nonenzymatic glucosylation, carbamylation, acetylation, ethylation, or methylation of lysine residues. Polyvalent or monoclonal antibodies that are absolutely specific for the lysine‐specific modification are obtained by immunization with modified autologous or homologous low‐density plasma lipoproteins.

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