精製ウサギγG抗体より分離したHeavyおよびLight Chainの抗体活性について : 第1報.間接赤血球凝集反応およびRadioimmunoelectrophoresisによる観察

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In order to assign the location of the antibody active sites, purified anti-DNP and anti-HAS rabbit γG antibodies were subjected to reduction and alkylation and their heavy and light polypeptide chains were separated by gel filtration. Subsequently, the reconstituents of heavy and light chains isolated from antibody molecules as well as the hybrid reconstituents of antibody polypeptide chains and normal γG counterparts were prepared. In comparison by radioimmunoelectrophoresis and passive hemagglutination of the antibody activity of these preparations, I.e. heavy chain, light chain and their specific or nonspecific (hybrid) reconstituents, following results were obtained. 1) Isolated light chains of anti-DNP or anti-HAS antibodies had no antibody activity. 2) On the contrary, isolated heavy chains obviously showed the antibody activity, though less active than original antibody γG. 3) Obvious enhancement of antibody activity of heavy chains was observed when they were combined with light chains derived from antibodies having same specificity. The enhancement is considered to be attributable to the reconstitution of heavy and light chains to form original γG molecules. 4) When light chains of normal γG globulin molecules were added to antibody heavy chains, the reconstitution of both chains into 7S γG globulin was observed to occur, but the activity of these reconstituents was the same as that of heavy chain alone. 5) The reconstituent consisting of normal heavy chain and antibody light chain did not show any antibody activities. 6) Reduction and alkylation of purified antibody without subsequent exposure to acid had little effect upon its antibody activities.
日本アレルギー学会の論文
1970-02-28

精製ウサギγG抗体より分離したHeavyおよびLight Chainの抗体活性について : 第1報.間接赤血球凝集反応およびRadioimmunoelectrophoresisによる観察

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