Evidence that the Ya and Yc Subunits of Glutathione Transferase B (Ligandin) are the Products of Separate Genes

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Abstract
A study of the structure of glutathione transferase B (ligandin) has been made with a view to understanding the relationship between the structures of the subunits of which it is composed. It consists of a mixture of a homodimer (Ya Ya) and a heterodimer (Ya Yc) in which the monomers are denned by their apparent molecular weights, that of Ya being 22000 and Yc 25000. Soluble tryptic peptides from the native homodimer Ya Ya have been compared with those from an artificial homodimer Yc Yc produced by rehybridization of native Ya Yc. Approximately 10 peptides specific to Ya Ya, 12 specific to Yc Yc and 21 common to both have been detected. Some of the above peptides are derived from variants of the monomers themselves. Ya Ya and Yc Yc have two C termini which are the same in both dimers, namely phenylalanine and lysine. Also there are four cysteinyl peptides, of which three are common to Ya Ya and Yc Yc and one specific to each. These results suggest that Ya and Yc are derived from at least two different but related genes.