Interaction of C3 and C3b with immunoglobulin G

Research output: Contribution to journalArticle

36 Citations (Scopus)

Abstract

Human C3b as well as native C3 were found to bind to solid phase human and rabbit IgG. Haemolytically active C3 had significantly higher binding capacity to IgG than the C3b fragment. Inhibition experiments proved that C3 and C3b have common binding sites on the Fab and Fc part of the IgG molecule but the character of these binding sites was different. As a functional consequence of C3-IgG interaction, C3 binding was found to inhibit the specific precipitation of an IgG antibody preparation.

Original languageEnglish
Pages (from-to)805-810
Number of pages6
JournalMolecular Immunology
Volume20
Issue number8
DOIs
Publication statusPublished - 1983

Fingerprint

Immunoglobulin G
Binding Sites
Rabbits
Antibodies

ASJC Scopus subject areas

  • Molecular Biology
  • Immunology

Cite this

Interaction of C3 and C3b with immunoglobulin G. / Kulics, Judit; Rajnavolgyi, E.; Füst, G.; Gergely, J.

In: Molecular Immunology, Vol. 20, No. 8, 1983, p. 805-810.

Research output: Contribution to journalArticle

@article{7e6b13422fc8454c8bb5cd73908a5b5b,
title = "Interaction of C3 and C3b with immunoglobulin G",
abstract = "Human C3b as well as native C3 were found to bind to solid phase human and rabbit IgG. Haemolytically active C3 had significantly higher binding capacity to IgG than the C3b fragment. Inhibition experiments proved that C3 and C3b have common binding sites on the Fab and Fc part of the IgG molecule but the character of these binding sites was different. As a functional consequence of C3-IgG interaction, C3 binding was found to inhibit the specific precipitation of an IgG antibody preparation.",
author = "Judit Kulics and E. Rajnavolgyi and G. F{\"u}st and J. Gergely",
year = "1983",
doi = "10.1016/0161-5890(83)90076-7",
language = "English",
volume = "20",
pages = "805--810",
journal = "Molecular Immunology",
issn = "0161-5890",
publisher = "Elsevier Limited",
number = "8",

}

TY - JOUR

T1 - Interaction of C3 and C3b with immunoglobulin G

AU - Kulics, Judit

AU - Rajnavolgyi, E.

AU - Füst, G.

AU - Gergely, J.

PY - 1983

Y1 - 1983

N2 - Human C3b as well as native C3 were found to bind to solid phase human and rabbit IgG. Haemolytically active C3 had significantly higher binding capacity to IgG than the C3b fragment. Inhibition experiments proved that C3 and C3b have common binding sites on the Fab and Fc part of the IgG molecule but the character of these binding sites was different. As a functional consequence of C3-IgG interaction, C3 binding was found to inhibit the specific precipitation of an IgG antibody preparation.

AB - Human C3b as well as native C3 were found to bind to solid phase human and rabbit IgG. Haemolytically active C3 had significantly higher binding capacity to IgG than the C3b fragment. Inhibition experiments proved that C3 and C3b have common binding sites on the Fab and Fc part of the IgG molecule but the character of these binding sites was different. As a functional consequence of C3-IgG interaction, C3 binding was found to inhibit the specific precipitation of an IgG antibody preparation.

UR - http://www.scopus.com/inward/record.url?scp=0020609662&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020609662&partnerID=8YFLogxK

U2 - 10.1016/0161-5890(83)90076-7

DO - 10.1016/0161-5890(83)90076-7

M3 - Article

C2 - 6621540

AN - SCOPUS:0020609662

VL - 20

SP - 805

EP - 810

JO - Molecular Immunology

JF - Molecular Immunology

SN - 0161-5890

IS - 8

ER -