Hybridization between the Heterologous Chains of Native Ricin D and Iodinated or Maleyl Ricin D

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Abstract
Two constituent polypeptide chains of native or iodinated ricin D were separated by affinity chromatography on Sepharose 4B after reduction with β-mercaptoethanol, and purified by DEAE-cellulose column chromatography. The hybrid molecule between the native lie chain and the iodinated Ala chain was easily formed by reduction-reoxidation of a mixture of both isolated chains. Its toxicity to mice was about 20 % of that of ricin D and about ten fold that of the iodinated ricin D. On the other hand, the hybrid molecule between native Ala chain and maleyl lie chain was obtained by reduction-reoxidation of a mixture of native and maleyl ricin D, and its toxicity to mice was about 15 % of that of ricin D and about four fold that of maleyl ricin D. These results suggest that tyrosine and lysine residues in each chain of ricin D are involved in the toxic action of ricin D.