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Article

A genetically engineered human IgG mutant with enhanced cytolytic activity

1 May 1992

Abstract excerpt

A mutant chimeric anti-5-dimethylaminonaphthalene-1-sulfonyl human Ig gamma that exhibited augmented effector function was constructed. Utilizing directed mutagenesis, a serine residue near the carboxyl terminus of the human IgG1 H chain (Ser444) was replaced by a cysteine. Novel intermolecular disulfide bonds between Cys444 residues linked pairs of Ig "tail-to-tail" to form covalent dimers ((H2L2)2). These...

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Identifiers

PMID: 1573276
DOI: 10.4049/jimmunol.148.9.2918

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