The actions of glutathione S-transferase and tyrosinase on the in vitro production of glutathionyl-3,4-dihydroxyphenylalanine and the dopachrome level in the presence of GSH and L-3,4-dihydroxyphenylalanine were studied. No clear evidence of complementarity between tyrosinase and glutathione S-transferase was observed; on the contrary, in the presence of glutathione S-transferase the glutathionyl-3,4-dihydroxyphenylalanine yield was lower than with tyrosinase only, as measured by HPLC. It is concluded that the spontaneous conjugation of GSH with dopaquinone should probably be high enough to scavenge the toxic quinone and to produce precursors for phaeomelanogenesis.