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Structural Characterization of Mouse Monoclonal Antibody 13-1 Against a Porphyrin Derivative: Identification of a Disulfide Bond in CDR-H3 of Mab 13-1

S Akashi, K Kato, T Torizawa, N Dohmae, H Yamaguchi, M Kamachi, A Harada, T Imanaka, I Shimada, K Takio

Biochem Biophys Res Commun. 1997 Nov 26;240(3):566-72.

PMID: 9398605

Abstract:

The amino acid sequence of a mouse monoclonal antibody Mab13-1, a catalytic antibody against TCPP (meso-tetrakis(4-carboxyphenyl)porphyrin), was confirmed by mass spectrometric (MS) peptide mapping. The amino-terminal sequence of the heavy chain was established by MS/MS analysis of the isolated N-terminal peptide. The presence of a unique disulfide bond between Cys93H and Cys102H was identified by MS peptide mapping and sequence analysis of an S-S containing peptide. Positions of other disulfide bonds were identified to be conserved. The non-conserved disulfide bridge was found to be resistant as other intra-chain disulfide bonds against reduction under non-denaturing condition, and to be buried inside the molecule. This extra disulfide bond is expected to support antigen-binding by restricting the flexibility of CDR-H3 loop, and it might be favorable for the recognition of a plane antigen, a porphyrin derivative.

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