Localization and functional significance of a polymorphic determinant in the third component of human complement

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Localization and functional significance of a polymorphic determinant in the third component of human complement. / Behrendt, N; Hansen, O C; Ploug, M; Barkholt, V.; Koch, C.

I: Molecular Immunology, Bind 24, Nr. 10, 10.1987, s. 1097-103.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Behrendt, N, Hansen, OC, Ploug, M, Barkholt, V & Koch, C 1987, 'Localization and functional significance of a polymorphic determinant in the third component of human complement', Molecular Immunology, bind 24, nr. 10, s. 1097-103.

APA

Behrendt, N., Hansen, O. C., Ploug, M., Barkholt, V., & Koch, C. (1987). Localization and functional significance of a polymorphic determinant in the third component of human complement. Molecular Immunology, 24(10), 1097-103.

Vancouver

Behrendt N, Hansen OC, Ploug M, Barkholt V, Koch C. Localization and functional significance of a polymorphic determinant in the third component of human complement. Molecular Immunology. 1987 okt.;24(10):1097-103.

Author

Behrendt, N ; Hansen, O C ; Ploug, M ; Barkholt, V. ; Koch, C. / Localization and functional significance of a polymorphic determinant in the third component of human complement. I: Molecular Immunology. 1987 ; Bind 24, Nr. 10. s. 1097-103.

Bibtex

@article{c1aed560e6874d2b8347173348354cb6,
title = "Localization and functional significance of a polymorphic determinant in the third component of human complement",
abstract = "A polymorphic epitope in the third component of human complement was studied. This allotypic system is distinct from the electrophoretically determined C3 S/F polymorphism and is defined by the recognition of one allotype by a monoclonal antibody. Allotypic protein variants, C3F+ (reactive with this antibody) and C3S- (non-reactive with the antibody), were purified. Deglycosylation studies and N-terminal sequencing of CNBr fragments, reactive with the antibody, revealed that the polymorphic epitope was present in a beta chain fragment of mol. wt 20,000. In the intact C3 molecule, this fragment is situated with N-terminus at residue No. 202, using the numbering of the cDNA derived amino acid sequence of human prepro C3. Addition of Fab fragments from the alloselective antibody preferentially inhibited the activity of C3F+ in a haemolytic assay which is selective for the C3 activity in the alternative complement pathway.",
keywords = "Amino Acid Sequence, Antibodies, Monoclonal, Complement C3, Cyanogen Bromide, Electrophoresis, Polyacrylamide Gel, Epitopes, Humans, Peptide Fragments, Polymorphism, Genetic, Journal Article, Research Support, Non-U.S. Gov't",
author = "N Behrendt and Hansen, {O C} and M Ploug and V. Barkholt and C Koch",
year = "1987",
month = oct,
language = "English",
volume = "24",
pages = "1097--103",
journal = "Molecular Immunology",
issn = "0161-5890",
publisher = "Pergamon Press",
number = "10",

}

RIS

TY - JOUR

T1 - Localization and functional significance of a polymorphic determinant in the third component of human complement

AU - Behrendt, N

AU - Hansen, O C

AU - Ploug, M

AU - Barkholt, V.

AU - Koch, C

PY - 1987/10

Y1 - 1987/10

N2 - A polymorphic epitope in the third component of human complement was studied. This allotypic system is distinct from the electrophoretically determined C3 S/F polymorphism and is defined by the recognition of one allotype by a monoclonal antibody. Allotypic protein variants, C3F+ (reactive with this antibody) and C3S- (non-reactive with the antibody), were purified. Deglycosylation studies and N-terminal sequencing of CNBr fragments, reactive with the antibody, revealed that the polymorphic epitope was present in a beta chain fragment of mol. wt 20,000. In the intact C3 molecule, this fragment is situated with N-terminus at residue No. 202, using the numbering of the cDNA derived amino acid sequence of human prepro C3. Addition of Fab fragments from the alloselective antibody preferentially inhibited the activity of C3F+ in a haemolytic assay which is selective for the C3 activity in the alternative complement pathway.

AB - A polymorphic epitope in the third component of human complement was studied. This allotypic system is distinct from the electrophoretically determined C3 S/F polymorphism and is defined by the recognition of one allotype by a monoclonal antibody. Allotypic protein variants, C3F+ (reactive with this antibody) and C3S- (non-reactive with the antibody), were purified. Deglycosylation studies and N-terminal sequencing of CNBr fragments, reactive with the antibody, revealed that the polymorphic epitope was present in a beta chain fragment of mol. wt 20,000. In the intact C3 molecule, this fragment is situated with N-terminus at residue No. 202, using the numbering of the cDNA derived amino acid sequence of human prepro C3. Addition of Fab fragments from the alloselective antibody preferentially inhibited the activity of C3F+ in a haemolytic assay which is selective for the C3 activity in the alternative complement pathway.

KW - Amino Acid Sequence

KW - Antibodies, Monoclonal

KW - Complement C3

KW - Cyanogen Bromide

KW - Electrophoresis, Polyacrylamide Gel

KW - Epitopes

KW - Humans

KW - Peptide Fragments

KW - Polymorphism, Genetic

KW - Journal Article

KW - Research Support, Non-U.S. Gov't

M3 - Journal article

C2 - 2446123

VL - 24

SP - 1097

EP - 1103

JO - Molecular Immunology

JF - Molecular Immunology

SN - 0161-5890

IS - 10

ER -

ID: 178214776