Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the beta chain
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Antibodies against synthetic peptides representing the class-II antigen HLA-DR and -DQ beta chain N-terminal sequences were prepared in rabbits. The two octapeptides only share two amino acids and enzyme-linked immuno-assays showed the antisera only to bind to its own antigen. Both peptide antisera detected a 29 kDa component in immunoblots of Raji and AL-34 cell plasma membrane proteins separated by SDS gel electrophoresis. The binding of either N-terminal peptide antiserum was selectively inhibited only by the peptide used as antigen. Indirect immunofluorescence analysis by flow cytofluorometry showed specific surface immunofluorescence in 1:100-1:1000 dilutions in lymphoblastoid and blood mononucleated cells. In the latter the binding was primarily confined to monocytes and a subpopulation of lymphocytes. It is concluded that locus-specific immunological reagents to distinguish between beta chains of HLA-DR and -DQ have been prepared by the preparation by the production of antibodies against the N-terminal sequences of each polypeptide.
Original language | English |
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Journal | F E B S Letters |
Volume | 189 |
Issue number | 2 |
Pages (from-to) | 329-37 |
Number of pages | 9 |
ISSN | 0014-5793 |
Publication status | Published - 23 Sep 1985 |
- Amino Acid Sequence, Animals, Antibodies, Cell Line, Cell Transformation, Viral, Enzyme-Linked Immunosorbent Assay, Flow Cytometry, Fluorescent Antibody Technique, HLA-DQ Antigens, HLA-DR Antigens, Herpesvirus 4, Human, Histocompatibility Antigens Class II, Lymphocytes, Rabbits
Research areas
ID: 45575290