The Far Ultraviolet Optical Rotatory Dispersion, Circular Dichroism, and Absorption Spectra of a Myeloma Immunoglobulin, Immunoglobulin G

摘要: Abstract The optical rotatory properties of a myeloma globulin, immunoglobulin G (IgG), and normal individual IgG in the far ultraviolet were investigated by dispersion, circular dichroism, absorption spectroscopy. dispersion displayed two peaks, one at 205 mµ other 210 mµ, trough 228 lesser 230 deeper 198 mµ. γ-globulin peak 208 to acid media was suggestive formation right handed α helices both immunoglobulins. Circular dichroic analysis showed seven bands, 202 (+), 217 (-), 225 242 265 284 beginning negative band centered below 195 (≃192.5 mµ). Application Kronig-Kramers transform gave an curve compatible with obtained experimentally. peptide bond extinction, calculated from spectra, hypochromicity for analyses cleaved oxidative sulfitolysis disulfide bonds joining heavy light chains be essential maintenance certain electronic transitions present native protein. major transitions, however, appeared unaffected this treatment. Comparison Cotton effects sulfitolyzed product those whole molecule (pH 2.4) that these S—S are important restricting conformation change presence denaturing agent.