Molecular structural studies of effector functions of a mouse immunoglobulin G that lacks the entire CH1 domain: small-angle X-ray scattering, nanosecond fluorescence depolarization and stable isotope-aided NMR analyses.
Molecular structural studies are reported of a short-chain mouse IgG2a antibody that lacks the entire CH1 domain. We have recently shown that (1) this short-chain antibody comprises two components in which the inter light-chain disulfide bridge does and does not exist, and (2) these two components are different in the constitutive complement-activating activity [Mizutani et al. (1993) J. Immunol. 150, 131-138]. Structures were compared for these two components on the basis of small-angle X-ray scattering, nanosecond fluorescence depolarization and isotope-aided NMR data. It has been discussed how the presence and absence of the inter light-chain disulfide bridges affect the complement-activating activity of the two components of the short-chain antibody.
Mizutani
R
R
Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
Matsunaga
C
C
Kouyama
T
T
Sato
M
M
Katsube
Y
Y
Kato
K
K
Shimada
I
I
Arata
Y
Y
D000818:Animals; D002247:Carbon Isotopes; D003619:Dansyl Compounds; D005454:Fluorescence Polarization; D007127:Immunoglobulin Constant Regions; D007074:Immunoglobulin G / Q000737:chemistry*; D007143:Immunoglobulin Heavy Chains; D009682:Magnetic Resonance Spectroscopy; D051379:Mice; D011487:Protein Conformation; D012542:Scattering, Radiation; D014965:X-Rays
D002247:Carbon Isotopes; D003619:Dansyl Compounds; D007127:Immunoglobulin Constant Regions; D007074:Immunoglobulin G; D007143:Immunoglobulin Heavy Chains