Recombinant mouse monoclonal antibodies with single amino acid substitutions affecting Clq and high affinity Fc receptor binding have identical serum half-lives in the BALB/c mouse.

doi:10.1016/0161-5890(92)90103-5

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Article

Recombinant mouse monoclonal antibodies with single amino acid substitutions affecting Clq and high affinity Fc receptor binding have identical serum half-lives in the BALB/c mouse.

Molecular immunology - 1 Feb 1992

Wawrzynczak E J, Denham S, Parnell G D, Cumber A J, Jones P T, Winter G

Abstract excerpt

The serum half-lives of three recombinant mouse monoclonal antibodies, differing radically in their ability to bind to Clq or FcRI but only minimally in structure, were determined in the BALB/c mouse following intravenous administration. The wild-type antibody, a chimaeric antibody comprising variable domains binding 3-iodo-4-hydroxy-5-nitrophenylacetate and constant domains of the mouse IgG2b isotype, was...

Topics

Animals
Antibodies, Monoclonal
Complement Activating Enzymes
Female
Half-Life
Hyaluronan Receptors
Immunoglobulin G
Membrane Glycoproteins
Mice
Mice, Inbred BALB C

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mitochondrial Proteins

Mutation

Protein Engineering

Receptors, Complement

Receptors, Fc

Recombinant Proteins

Source

Open in PubMed

Identifiers

PMID: 1542299
DOI: 10.1016/0161-5890(92)90103-5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1542299-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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