FORMATION OF ACTIVE HYBRID IMMUNOGLOBULINS FROM HEAVY AND LIGHT-CHAINS OF BETA-(1, 6) D-GALACTAN BINDING MURINE MYELOMA IGAS S10 AND J539

  • 1 January 1977
    • journal article
    • research article
    • Vol. 119  (3) , 867-871
Abstract
Murine myeloma immunoglobulin (IgA, .kappa.) J539, which shows enhanced tryptophanyl fluorescence on ligand binding, and S10, which shows reverse-sign changes in tryptophanyl fluorescence on ligand binding, were reduced, alkylated and dissociated into their L and H chains. Two hybrid recombinants, H10L539 and H539L10, were prepared and the 7S material was isolated by chromatography. The binding behavior of these recombinants was studied with a number of ligands. Both recombinants showed activity with .beta.(1 .fwdarw. 6) linked galactose ligands comparable to the native Ig. The ligand-induced fluorescence changes of the recombinants paralleled those of the H chain donor. For the recombinant H10L539, 2 different galactose-ligands caused fluorescence changes in opposite directions. It was quantitatively shown that binding of these ligands took place in the same combining region. The idiotype of each recombinant resembled that of the H chain donor.

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