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J. Biochem, 1974, Vol. 76, No. 4 685-693
© 1974 Japanese Biochemical Society

research-article

Interactions between Immunoglobulin Polypeptide Chains*

Takachika AZUMA, Kozo HAMAGUCHI and Shunsuke MIGITA**

Department of Biology, Faculty of Science, Osaka University Toyonaka, Osaka
**Cancer Research Institute, Kanazawa University Kanazawa

  1. The dimerization of reduced and alkylated Bence Jones proteins was studied by gel chromatography and circular dichroic (CD) measurements. The association constants of two type {lambda} proteins, as estimated by gel chromatography, were 105 and 2×106 M–1 at pH 5.5, 25°C. The changes in the CD spectrum in the aromatic absorption region with protein concentration and those with pH on the alkaline side indicate that the monomeric and dimeric forms of type {lambda} proteins are different from each other as regards the environment of tyrosyl residues.
  2. The conformation of IgG molecules reconstituted from the alkylated H chain of a myeloma protein and various specimens of alkylated Bence Jones proteins was studied by CD measurements. The CD spectra of the recombinants were different depending on the specimens of L chains used, even if the antigenic type was the same. This indicates that the conformational change observed when H and L chains recombine is mainly associated with the conformational change of the variable portion of the L chain.

*1This work was supported in part by a scientific research grant from the Ministry of Education. The abbreviations for the immunoglobulins and their sub-units produced by reduction are those recommended by the World Health Organization (1964). Other abbreviations used in this paper are: CD, circular dichroism ; DTT, dithiothreitol.


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