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김하형(Ha Hyung Kim),이광표(Kwang Pyo Lee),Koichi Kato,Yoji Arata 대한약학회 1995 약학회지 Vol.39 No.5
The anti-dansyl antibodies were specifically labeled with stable isotope by growing hybridoma cells in serum-free medium. Assignments of the observed carbonyl carbon resonances have been determined by using 13C-15N double labeling method in order to assign the Leu resonances. However, when the identical dipeptide appears more than twice in the polypeptide sequences, we applied the proteolytic fragments in the fragment-specific method. Carboxypeptidase B-treated antibody has also been used to assign the Lys-447 in C terminal amino acid. These unambiguously assigned carbonyl carbon resonances in antibodies are thought to be useful in elucidating not only the structure of antibodies but also the structure-function relationship in the antibody by 13C neuclear magnetic resonance spectroscopy.
NMR에 의한 anti-Ex-A IgG의 항원결합부위 해석
김하형(Ha Hyung Kim),이광표(Kwang Pyo Lee),가토 코이치(Koichi Kato),아라타 요우지(Yoji Arata) 대한약학회 1996 약학회지 Vol.40 No.4
The anti-Ex-A IgG was specifically labeled with stable isotopes, DL-His-2,4-d2, L-Phe-d5, L-Trp-d5, L-Tyr-2,6-d2 and L-[1-13C]Trp, by growing hybridoma cell in serum-free medium. By use of NMR spectroscopy with selectively labeled Fab fragment, we applied a paratope mapping on antigen-antibody complex. Assignments of the observed carbonyl carbon resonances have been determined by using 13C-15N double labeling method in order to assign the Trp resonances. Photo CIDNP was also applied to investigate the antigen-binding site(s) on the surface residues of antibody. We found that Trp 36, which is located at the VH domain, is an important residue to bind to Ex-A, however, two Tyr on the surface of anti-Ex-A IgG plays no crucial role to bind to antigen. On the basis of these results, we demonstrate that stable isotope-aided NMR strategy can be extended to molecular structural analyses of the complex of an Fab fragment and a protein antigen.