Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the β chain

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Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the β chain. / Deufel, Thomas; Grove, Anne; Kofod, Hans; Lernmark, Åke.

In: FEBS Letters, Vol. 189, No. 2, 23.09.1985, p. 329-337.

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T1 - Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the β chain

AU - Deufel, Thomas

AU - Grove, Anne

AU - Kofod, Hans

AU - Lernmark, Åke

PY - 1985/9/23

Y1 - 1985/9/23

N2 - Antibodies against synthetic peptides representing the class-II antigen HLA-DR and -DQ β 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 β 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.

AB - Antibodies against synthetic peptides representing the class-II antigen HLA-DR and -DQ β 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 β 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.

KW - ELISA

KW - Flow cytofluorometry

KW - HLA class II antigen

KW - Immunoblotting bl]

UR - http://www.scopus.com/inward/record.url?scp=0021926776&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(85)81050-4

DO - 10.1016/0014-5793(85)81050-4

M3 - Article

C2 - 2995123

AN - SCOPUS:0021926776

VL - 189

SP - 329

EP - 337

JO - FEBS Letters

JF - FEBS Letters

SN - 1873-3468

IS - 2

ER -