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

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Standard

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

I: F E B S Letters, Bind 189, Nr. 2, 23.09.1985, s. 329-37.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Deufel, T, Grove, A, Kofod, H & Lernmark, A 1985, 'Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the beta chain', F E B S Letters, bind 189, nr. 2, s. 329-37.

APA

Deufel, T., Grove, A., Kofod, H., & Lernmark, A. (1985). Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the beta chain. F E B S Letters, 189(2), 329-37.

Vancouver

Deufel T, Grove A, Kofod H, Lernmark A. Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the beta chain. F E B S Letters. 1985 sep. 23;189(2):329-37.

Author

Deufel, T ; Grove, A ; Kofod, Hans ; Lernmark, A. / Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the beta chain. I: F E B S Letters. 1985 ; Bind 189, Nr. 2. s. 329-37.

Bibtex

@article{5d5c50dc5fe84274a676da11242cb3d8,
title = "Locus-specific detection of HLA-DQ and -DR antigens by antibodies against synthetic N-terminal octapeptides of the beta chain",
abstract = "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.",
keywords = "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",
author = "T Deufel and A Grove and Hans Kofod and A Lernmark",
year = "1985",
month = sep,
day = "23",
language = "English",
volume = "189",
pages = "329--37",
journal = "F E B S Letters",
issn = "0014-5793",
publisher = "JohnWiley & Sons Ltd",
number = "2",

}

RIS

TY - JOUR

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

AU - Deufel, T

AU - Grove, A

AU - Kofod, Hans

AU - Lernmark, A

PY - 1985/9/23

Y1 - 1985/9/23

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Antibodies

KW - Cell Line

KW - Cell Transformation, Viral

KW - Enzyme-Linked Immunosorbent Assay

KW - Flow Cytometry

KW - Fluorescent Antibody Technique

KW - HLA-DQ Antigens

KW - HLA-DR Antigens

KW - Herpesvirus 4, Human

KW - Histocompatibility Antigens Class II

KW - Lymphocytes

KW - Rabbits

M3 - Journal article

C2 - 2995123

VL - 189

SP - 329

EP - 337

JO - F E B S Letters

JF - F E B S Letters

SN - 0014-5793

IS - 2

ER -

ID: 45575290