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PMID: 10698313 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Sedimentation equilibrium analysis of recombinant mouse FcRn with murine IgG1.

Molecular immunology ·Vol. 36 ·No. 15-16 ·1999-00-00 ·Pages 1117-25

Schuck P, Radu CG, Ward ES

Abstract

The interaction of mouse IgG1 or IgG1-derived Fc fragment with recombinant, insect cell expressed mouse FcRn has been analyzed using sedimentation equilibrium. This results in a model for the interaction in which the two binding sites for FcRn on Fc or IgG1 have significantly different affinities with macroscopic binding constants of < 130 nM and 6 microM. This data indicates the formation of an asymmetric FcRn:Fc (or IgG1):FcRn complex which is consistent with earlier suggestions that for this form of recombinant FcRn, binding to IgG1 or Fc does not result in a symmetric 2:1 complex in which both binding sites are equivalent.

MeSH Terms
Animals Antibody Affinity Binding Sites Histocompatibility Antigens Class I Immunoglobulin Fc Fragments/isolation & purification,metabolism Immunoglobulin G/isolation & purification,metabolism In Vitro Techniques Kinetics Mice Receptors, Fc/isolation & purification,metabolism Recombinant Proteins/isolation & purification,metabolism Ultracentrifugation
Chemicals
Histocompatibility Antigens Class I Immunoglobulin Fc Fragments Immunoglobulin G Receptors, Fc Recombinant Proteins Fc receptor, neonatal
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Schuck P
Molecular Interactions Resource ORS, Bioengineering and Physical Science Program, National Institutes of Health, Bethesda, MD 20892-5766, USA.
Radu C G
Ward E S
Article Info
Journal
Molecular immunology
Abbr.
Mol Immunol
ISSN
0161-5890
Published
1999-00-00
Pages
1117-25
Language
English
Region
England
NLM ID
7905289
Subset
IM
Grants
NIAID NIH HHS · R01 AI39167 · United States
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