RECOMBINATION OF HEAVY AND LIGHT CHAINS OF HUMAN γA-MYELOMA PROTEINS: FORMATION OF HYBRID MOLECULES AND CONFIGURATIONAL SPECIFICITY

Abstract

The present studies demonstrate that the conditions necessary for reductive cleavage, isolation, and recombination of L and H polypeptide chains of human γA-myeloma globulins parallel those required for similar manipulation of the component chains of γG-globulin. Specificity of recombination was shown for chains derived from the same protein. In contrast, no intradass preferential recombination was demonstrable.