Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules

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Standard

Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules. / Petersen, J S; Atar, D; Karlsen, Alan E; Kofod, Hans; Dyrberg, T.

I: Biomedica Biochimica Acta, Bind 49, Nr. 12, 1990, s. 1223-32.

Publikation: Bidrag til tidsskriftTidsskriftartikelForskningfagfællebedømt

Harvard

Petersen, JS, Atar, D, Karlsen, AE, Kofod, H & Dyrberg, T 1990, 'Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules', Biomedica Biochimica Acta, bind 49, nr. 12, s. 1223-32.

APA

Petersen, J. S., Atar, D., Karlsen, A. E., Kofod, H., & Dyrberg, T. (1990). Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules. Biomedica Biochimica Acta, 49(12), 1223-32.

Vancouver

Petersen JS, Atar D, Karlsen AE, Kofod H, Dyrberg T. Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules. Biomedica Biochimica Acta. 1990;49(12):1223-32.

Author

Petersen, J S ; Atar, D ; Karlsen, Alan E ; Kofod, Hans ; Dyrberg, T. / Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules. I: Biomedica Biochimica Acta. 1990 ; Bind 49, Nr. 12. s. 1223-32.

Bibtex

@article{7ed1cce21b204656b52d1edae48f1e40,
title = "Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules",
abstract = "In an attempt to produce epitope specific antisera which could distinguish two closely associated HLA-DQ beta-chain alleles, we immunized 20 rabbits with synthetic peptides representing sequences from the first domain of the HLA-DQw8 and -DQw7 beta-chain molecules, differing only by one amino acid in position 57. Several of the antisera in immunoblotting specifically recognized either the HLA-DQw7 or the HLA-DQw8 beta-chain allele as previously reported. The fine specificity of the antisera was tested in ELISA using synthetic peptides of varying length as solid phase antigen. Two out of the 20 antisera specifically recognized DQw7 beta peptides and two antisera bound only to DQw8 beta peptides from the region containing the amino acid in position 57. To analyze whether the antisera bound to native HLA-DQ beta-chain molecules, FACS analysis was carried out. Seven of the 20 antisera bound to intact EBV-transformed B-lymphocytes, and one antiserum bound preferentially to HLA-DQw8 positive cells.",
keywords = "Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, Enzyme-Linked Immunosorbent Assay, Epitopes, Flow Cytometry, HLA-DQ Antigens, Immune Sera, Molecular Sequence Data, Peptides, Rabbits",
author = "Petersen, {J S} and D Atar and Karlsen, {Alan E} and Hans Kofod and T Dyrberg",
year = "1990",
language = "English",
volume = "49",
pages = "1223--32",
journal = "Biomedica Biochimica Acta",
issn = "0232-766X",
publisher = "Akademie Verlag GMBH",
number = "12",

}

RIS

TY - JOUR

T1 - Characterization of the fine specificity of peptide antibodies to HLA-DQ beta-chain molecules

AU - Petersen, J S

AU - Atar, D

AU - Karlsen, Alan E

AU - Kofod, Hans

AU - Dyrberg, T

PY - 1990

Y1 - 1990

N2 - In an attempt to produce epitope specific antisera which could distinguish two closely associated HLA-DQ beta-chain alleles, we immunized 20 rabbits with synthetic peptides representing sequences from the first domain of the HLA-DQw8 and -DQw7 beta-chain molecules, differing only by one amino acid in position 57. Several of the antisera in immunoblotting specifically recognized either the HLA-DQw7 or the HLA-DQw8 beta-chain allele as previously reported. The fine specificity of the antisera was tested in ELISA using synthetic peptides of varying length as solid phase antigen. Two out of the 20 antisera specifically recognized DQw7 beta peptides and two antisera bound only to DQw8 beta peptides from the region containing the amino acid in position 57. To analyze whether the antisera bound to native HLA-DQ beta-chain molecules, FACS analysis was carried out. Seven of the 20 antisera bound to intact EBV-transformed B-lymphocytes, and one antiserum bound preferentially to HLA-DQw8 positive cells.

AB - In an attempt to produce epitope specific antisera which could distinguish two closely associated HLA-DQ beta-chain alleles, we immunized 20 rabbits with synthetic peptides representing sequences from the first domain of the HLA-DQw8 and -DQw7 beta-chain molecules, differing only by one amino acid in position 57. Several of the antisera in immunoblotting specifically recognized either the HLA-DQw7 or the HLA-DQw8 beta-chain allele as previously reported. The fine specificity of the antisera was tested in ELISA using synthetic peptides of varying length as solid phase antigen. Two out of the 20 antisera specifically recognized DQw7 beta peptides and two antisera bound only to DQw8 beta peptides from the region containing the amino acid in position 57. To analyze whether the antisera bound to native HLA-DQ beta-chain molecules, FACS analysis was carried out. Seven of the 20 antisera bound to intact EBV-transformed B-lymphocytes, and one antiserum bound preferentially to HLA-DQw8 positive cells.

KW - Amino Acid Sequence

KW - Animals

KW - Carrier Proteins

KW - Cell Line

KW - Enzyme-Linked Immunosorbent Assay

KW - Epitopes

KW - Flow Cytometry

KW - HLA-DQ Antigens

KW - Immune Sera

KW - Molecular Sequence Data

KW - Peptides

KW - Rabbits

M3 - Journal article

C2 - 1711320

VL - 49

SP - 1223

EP - 1232

JO - Biomedica Biochimica Acta

JF - Biomedica Biochimica Acta

SN - 0232-766X

IS - 12

ER -

ID: 45574926