Biopolym. Cell. 1989; 5(4):37-45.
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


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.


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