In:
European Journal of Immunology, Wiley, Vol. 9, No. 1 ( 1979-01), p. 91-93
Abstract:
The effect of antibodies to the light chain variable region (V L ) of protein MOPC‐315 (a, Λ 2 ), on the binding of hapten by V L 315 dimer or Fv315 (V L + V H ) was studied by equilibrium dialysis. Anti‐V L did not change the binding properties of Fv but affected the binding properties of V L dimer. At pH 5, the binding properties of V L in the presence or absence of anti‐V L were the same, whereas at pH 8, anti‐V L reduced the number of ligands bound to V L from two to one. It has previously been shown that V L dimer binds one ligand at pH 5 and two ligands at pH 8, and that V L conformation at pH 5 is tighter. Hence, our results suggest that anti‐V L tightens the conformation of V L dimer at pH 8.0 such that it can bind only one ligend. Since Fv is not affected by anti‐V L , the results indicate that a combining site made of two identical chains (V L dimer) can undergo a conformational change upon interaction with its antibody. Such conformational change can indirectly affect the binding properties.
Type of Medium:
Online Resource
ISSN:
0014-2980
,
1521-4141
DOI:
10.1002/eji.1830090119
Language:
English
Publisher:
Wiley
Publication Date:
1979
detail.hit.zdb_id:
1491907-2
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