Luminescence studies on Bence--Jones proteins and light chains of immunoglobulins and their subunits

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

参考文章(23)
Carla L. McLaughlin, Alan Solomon, Bence-Jones Proteins and Light Chains of Immunoglobulins Journal of Biological Chemistry. ,vol. 247, pp. 5017- 5025 ,(1972) , 10.1016/S0021-9258(19)44933-8
C. Milstein, J.R.L. Pink, Structure and evolution of immunoglobulins Progress in Biophysics & Molecular Biology. ,vol. 21, pp. 209- 263 ,(1970) , 10.1016/0079-6107(70)90026-X
A. B. Edmundson, K. R. Ely, E. E. Abola, M. Schiffer, N. Panagiotopoulos, Rotational allomerism and divergent evolution of domains in immunoglobulin light chains Biochemistry. ,vol. 14, pp. 3953- 3961 ,(1975) , 10.1021/BI00689A005
Peter M. Colman, Johann Deisenhofer, Robert Huber, Walter Palm, Structure of the human antibody molecule kol (immunoglobulin G1): An electron density map at 5 Å resolution Journal of Molecular Biology. ,vol. 100, pp. 257- 278 ,(1976) , 10.1016/S0022-2836(76)80062-9
R. J. Poljak, L. M. Amzel, H. P. Avey, B. L. Chen, R. P. Phizackerley, F. Saul, Three-Dimensional Structure of the Fab′ Fragment of a Human Immunoglobulin at 2.8-Å Resolution Proceedings of the National Academy of Sciences of the United States of America. ,vol. 70, pp. 3305- 3310 ,(1973) , 10.1073/PNAS.70.12.3305
Gerald M. Edelman, Covalent structure of a human γG-immunoglobulin. XI. Functional implications Biochemistry. ,vol. 9, pp. 3197- 3205 ,(1970) , 10.1021/BI00818A012
D. M. Segal, E. A. Padlan, G. H. Cohen, S. Rudikoff, M. Potter, D. R. Davies, The Three-Dimensional Structure of a Phosphorylcholine-Binding Mouse Immunoglobulin Fab and the Nature of the Antigen Binding Site Proceedings of the National Academy of Sciences of the United States of America. ,vol. 71, pp. 4298- 4302 ,(1974) , 10.1073/PNAS.71.11.4298
Marianne Schiffer, Rowland L. Girling, Kathryn R. Ely, Allen B. Edmundson, Structure of a lambda-type Bence-Jones protein at 3.5-A resolution. Biochemistry. ,vol. 12, pp. 4620- 4631 ,(1972) , 10.1021/BI00747A013