作者: James W. Longworth , Carla L. McLaughlin , Alan Solomon
DOI: 10.1021/BI00659A003
关键词:
摘要: To provide information on the tertiary structure of antibody molecule we have investigated luminescent properties light polypeptide chain human immunoglobulins. The fluorescence and phosphorescence yields, spectra, lifetimes, anisotropies a large number homogeneous chains, i.e., Bence--Jones proteins chains derived from myeloma proteins, were measured. No two gave identical tyrosyl or tryptophyl spectra in comparative studies over 75 belonging to four basic subgroups kappa lambda chains. Spectral differences apparent even among exhibiting more than 85 percent amino acid sequence identity. yields tyrosine tryptophan varied 10- 100-fold, respectively; Stokes' shift ranged 328 365 nm, but that for was apparently invariant (305 307 nm). Emission as well excitation showed residues interact minimally not at all. Fluorescence lifetimes contributions measured separately, natural calculated. Proteins could be grouped accordance with similarities yields; there no evident relationship between these groupings type (kappa lambda), aminomore » sequence, content.« less