Preparation and characterization of antibodies to the λ chain variable region (Vλ) of mouse immunoglobulins

Y. Ben‐Neriah*, P. Lonai, M. Gavish, D. Givol

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

20 Scopus citations

Abstract

The variable portion (VL) of the mouse myeloma protein MOPC‐315 (α, λ2) was obtained from its Fv fragment and was used to immunize rabbits. Anti‐VL antibodies were found to be specific to the VL region of protein 315 and to precipitate VL, Fv or light chain but not Fab' or intact M315. Anti‐VL 315 precipitates also the light chain of MOPC‐104E (μ, λ1) but not the intact protein. Intact immunoglobulins (Ig) containing λ chains, although they do not precipitate with anti‐VL, inhibit the binding of anti‐VL to VL in the radioimmunoassay. Radioimmunoassay inhibition studies demonstrated that Vλ1 and Vλ2 cross‐react extensively and that anti‐VL 315 can be used as a general anti‐Vλ reagent to detect molecules containing λ chains in mouse serum. Analysis of sera from several mouse strains indicated that Vλ‐containing molecules are present in approximately 3% of the Ig population, whereas the SJL strain has no detectable Vλ‐bearing molecules. In some of the antisera, anti‐VL 315 slightly cross‐reacted with VK‐bearing molecules. Anti‐VL 315 antibodies are not anti‐idiotypes since they react with myeloma proteins M315 (anti‐2,4‐dinitrophenyl MOPC‐104E (anti‐dextran) and HOPC‐1 (specificity unknown) and with most serum Ig containing λ chains. In view of the similarity of mouse λ chain sequences, it is suggested that most anti‐VL 315 is “anti‐framework” antibody.

Original languageAmerican English
Pages (from-to)792-796
Number of pages5
JournalEuropean Journal of Immunology
Volume8
Issue number11
DOIs
StatePublished - Nov 1978

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