Anti‐V region framework antibodies affect the ligand binding of VL dimer

Yinon Ben‐Neriah, David Givol*, Moshe Gavish

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review


The effect of antibodies to the light chain variable region (VL) of protein MOPC‐315 (a, Λ2), on the binding of hapten by VL315 dimer or Fv315 (VL + VH) was studied by equilibrium dialysis. Anti‐VL did not change the binding properties of Fv but affected the binding properties of VL dimer. At pH 5, the binding properties of VL in the presence or absence of anti‐VL were the same, whereas at pH 8, anti‐VL reduced the number of ligands bound to VL from two to one. It has previously been shown that VLdimer binds one ligand at pH 5 and two ligands at pH 8, and that VL conformation at pH 5 is tighter. Hence, our results suggest that anti‐VL tightens the conformation of VL dimer at pH 8.0 such that it can bind only one ligend. Since Fv is not affected by anti‐VL, the results indicate that a combining site made of two identical chains (VLdimer) can undergo a conformational change upon interaction with its antibody. Such conformational change can indirectly affect the binding properties.

Original languageAmerican English
Pages (from-to)91-93
Number of pages3
JournalEuropean Journal of Immunology
Issue number1
StatePublished - Jan 1979


Dive into the research topics of 'Anti‐V region framework antibodies affect the ligand binding of VL dimer'. Together they form a unique fingerprint.

Cite this