A 13C NMR study of the hinge region of a mouse monoclonal antibody.
A 13C NMR study is reported of the hinge region of an intact mouse monoclonal antibody with a molecular weight of 150 K. Cys, Ile, and Pro analogs of the antibody labeled with 13C at the carbonyl carbon were prepared by growing hybridoma cells in the serum-free media. Resonance assignments have been performed as described previously [Kato, K., Matsunaga, C., Igarashi, T., Kim, H., Odaka, A., Shimada, I. and Arata, Y. (1991) Biochemistry, 30, 270-278]. The spectral data obtained show that 13C NMR can give detailed information about the structure of the hinge region of the intact antibody molecule. Prospects for the future role of 13C NMR in the structural analyses of larger proteins are briefly discussed.
Matsunaga
C
C
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Kato
K
K
Arata
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal / Q000737:chemistry*; D002247:Carbon Isotopes; D002460:Cell Line; D007140:Immunoglobulin Fab Fragments / Q000737:chemistry; D007141:Immunoglobulin Fc Fragments / Q000737:chemistry; D007074:Immunoglobulin G / Q000737:chemistry* / Q000145:classification; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D051379:Mice; D008969:Molecular Sequence Data; D009587:Nitrogen Isotopes; D011487:Protein Conformation
D000911:Antibodies, Monoclonal; D002247:Carbon Isotopes; D007140:Immunoglobulin Fab Fragments; D007141:Immunoglobulin Fc Fragments; D007074:Immunoglobulin G; D009587:Nitrogen Isotopes