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Article

Engineering an improved IgG4 molecule with reduced disulfide bond heterogeneity and increased Fab domain thermal stability.

The Journal of biological chemistry - 13 Jul 2012

Peters Shirley J, Smales C Mark, Henry Alistair J, Stephens Paul E, West Shauna, Humphreys David P

Abstract excerpt

The integrity of antibody structure, stability, and biophysical characterization are becoming increasingly important as antibodies receive increasing scrutiny from regulatory authorities. We altered the disulfide bond arrangement of an IgG4 molecule by mutation of the Cys at the N terminus of the heavy chain constant domain 1 (C(H)1) (Kabat position 127) to a Ser and introduction of a Cys at a variety of...

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Identifiers

PMID: 22610095
DOI: 10.1074/jbc.M112.369744
PMCID: PMC3397877

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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