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Free radical research, 1996-01, Vol.25 (2), p.149-159
1996

Details

Autor(en) / Beteiligte
Titel
Monoclonal Antibodies for Detection of 4-Hydroxynonenal Modified Proteins
Ist Teil von
  • Free radical research, 1996-01, Vol.25 (2), p.149-159
Ort / Verlag
England: Informa UK Ltd
Erscheinungsjahr
1996
Link zum Volltext
Quelle
Taylor & Francis Journals Auto-Holdings Collection
Beschreibungen/Notizen
  • A promising approach to study lipid peroxidation pathology is antibodies recognizing aldehydes which react with and became bound to amino acid side chains of proteins. We present in this study the characterization of several monoclonal antibodies which recognize 4-hydroxynonenal (HNE) modified proteins. Six out of 20 antibodies recognizing HNE modified BSA were able to detect HNE-protein adducts in peroxidized liver microsomes. Two of these antibodies were selected and characterized. Both antibodies could also detect HNE-protein adducts in oxidized low density lipoprotein. They exhibit no detectable cross reaction with proteins modified by malonaldehyde, nonanal, nonenal and 4-hydroxyhexenal. Protein bound 4-hydroxyoctenal and 4-hydroxydecenal were recognized to some extent. Further characterization revealed that the two antibodies are highly selective for HNE bound to histidine with only some cross reaction to HNE bound to lysine and cysteine. Preliminary quantitative ELISA-analysis showed that oxidized microsomes and oxidized LDL contain 12 nmol and 3 nmol HNE-histidine per mg protein respectively.

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