Biopolym. Cell. 1989; 5(4):37-45.
http://dx.doi.org/10.7124/bc.0000D1
Structure and Function of Biopolymers
Constant domain epitope expression of human immunoglobulin L chains of the κ and λ type in proteins of different variable subgroups
1Rokhlin O. V., 2Solomon A., 2Vasse D., 1Ibragimov A. R., 1Arsenieva E. L., 1Bogacheva G. T.
  1. Research Institute of Experimental Cardiology, National Cardiological Research Centre, Academy of Medical Sciences of the USSR
    Moscow, USSR
  2. Department of Medicine, University of Tennessee, Knoxville
    Tennessee, USA

Abstract

Monoclonal antibodies against three different κ-chain constant domain epitopes and three different human Ig λ-chain C-domain epitopes have been prepared. Some of the epitopes are expressed both in intact Ig molecules and in isolated L-chains, whereas other epitopes are found only in isolated λ-chains. The expression of these epitopes has been studied in 40 various myeloma κ-chain preparations belonging to four different variable subgroups, and in 52 λ-chain preparations of three V subgroups. The expression level in the above epitope of C domain is shown to depend on the variable subgroups of L-chains. This implies the existence of certain interactions between V and C domains promoting the alteration in the level of C domain epitope expression. These studies indicate that interactions of structurally distinct V domains with the C domain probably lead to local conformational changes of the C domain.
Full text: (PDF, in Russian)

References

[1] Solomon A. Light chains of immunoglobulins: structural-genetic correlates. Blood. 1986;68(3):603-10.
[2] Hieter PA, Hollis GF, Korsmeyer SJ, Waldmann TA, Leder P. Clustered arrangement of immunoglobulin lambda constant region genes in man. Nature. 1981;294(5841):536-40.
[3] Chang H, Dmitrovsky E, Hieter PA, Mitchell K, Leder P, Turoczi L, Kirsch IR, Hollis GF. Identification of three new Ig lambda-like genes in man. J Exp Med. 1986;163(2):425-35.
[4] Ling NR, Lowe J, Hardie D, Evans S, Jefferis R. Detection of free kappa chains in human serum and urine using pairs of monoclonal antibodies reacting with C kappa epitopes not available on whole immunoglobulins. Clin Exp Immunol. 1983;52(1):234-40.
[5] Walker LC, Dhut S, Gregory WM, Habeshaw JA. Cross-reactive variable-region associated epitopes of human IgG1 lambda paraprotein detected by a monoclonal antibody panel. Immunology. 1987;61(3):247-54.
[6] Solomon A. Bence Jones proteins and light chains of immunoglobulins. XIV. Conformational dependency and molecular localization of the kappa (kappa) and lambda (lambda) antigenic determinants. Scand J Immunol. 1976;5(6-7):685-95.
[7] Solomon A. Light chains of human immunoglobulins. Methods Enzymol. 1985;116:101-21.
[8] Silverman GJ, Carson DA, Solomon A, Fong S. Human kappa light chain subgroup analysis with synthetic peptide-induced antisera. J Immunol Methods. 1986;95(2):249-57.
[9] Solomon A, Weiss DT. Serologically defined V region subgroups of human lambda light chains. J Immunol. 1987;139(3):824-30.
[10] Kearney JF, Radbruch A, Liesegang B, Rajewsky K. A new mouse myeloma cell line that has lost immunoglobulin expression but permits the construction of antibody-secreting hybrid cell lines. J Immunol. 1979;123(4):1548-50.
[11] Kohler G, Milstein C. Continuous cultures of fused cells secreting antibody of predefined specificity. Nature. 1975;256(5517):495-7.
[12] Cherapakhin VV, Chervonsky AV, Filatov AV, Rokhlin OV. Monoclonal antibodies against common and Igk-1a allotypic determinants of rat immunoglobulin kappa chain constant domain. Immunol Lett. 1985;10(3-4):217-21.
[13] Carlsson J, Drevin H, Axen R. Protein thiolation and reversible protein-protein conjugation. N-Succinimidyl 3-(2-pyridyldithio)propionate, a new heterobifunctional reagent. Biochem J. 1978;173(3):723-37.
[14] Gurevich AE, Kuzovleva OB, Tumanova AE. Production of protein-cellulose complexes (immunosorbents) in suspension forms with the capacity for absorption of large amounts of antibodies. Biokhimiia. 1961;26:934-42.
[15] Alzari PM, Lascombe MB, Poljak RJ. Three-dimensional structure of antibodies. Annu Rev Immunol. 1988;6:555-80.
[16] Schiffer M, Girling RL, Ely KR, Edmundson AB. Structure of a lambda-type Bence-Jones protein at 3.5-A resolution. Biochemistry. 1973;12(23):4620-31.
[17] Alexandru I, Kells DI, Dorrington KJ, Klein M. Non-covalent association of heavy and light chains of human immunoglobulin G: studies using light chain labelled with a fluorescent probe. Mol Immunol. 1980;17(11):1351-63.
[18] Edmundson AB, Ely KR, Herron JN. A search for site-filling ligands in the Mcg Bence-Jones dimer: crystal binding studies of fluorescent compounds. Mol Immunol. 1984;21(7):561-76.
[19] Klein M, Kortan C, Kells DI, Dorrington KJ. Equilibrium and kinetic aspects of the interaction of isolated variable and constant domains of light chain with the Fd' fragment of immunoglobulin G. Biochemistry. 1979;18(8):1473-81.
[20] Solomon A, McLaughlin CL, Steinberg AG. Bence Jones proteins and light chains of immunoglobulins. 3. Inv antigenicity: a genetic expression with serologic dependency of the intact kappa light chain molecule. Immunochemistry. 1970;7(8):709-13.