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.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Antibody Affinity
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Binding Sites
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Histocompatibility Antigens Class I
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Immunoglobulin Fc Fragments / isolation & purification
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Immunoglobulin Fc Fragments / metabolism
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Immunoglobulin G / isolation & purification
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Immunoglobulin G / metabolism*
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In Vitro Techniques
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Kinetics
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Mice
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Receptors, Fc / isolation & purification
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Receptors, Fc / metabolism*
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Recombinant Proteins / isolation & purification
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Recombinant Proteins / metabolism
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Ultracentrifugation
Substances
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Histocompatibility Antigens Class I
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Immunoglobulin Fc Fragments
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Immunoglobulin G
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Receptors, Fc
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Recombinant Proteins
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Fc receptor, neonatal