Decreased activity of uroporphyrinogen decarboxylase caused by 2,4,5,3',4'-pentabromobiphenyl in chick embryo hepatocyte cultures. Difference in activity in intact or homogenized cells.

Uroporphyrinogen decarboxylase activity was investigated in cultures of chick embryo liver by two different methods: (1) analysis of porphyrin composition following incubation of intact cells with delta-aminolevulinic acid; and (2) a more conventional direct enzymic assay of cell homogenates. Activity was detectibly decreased following exposure of cells to 100 ng/ml 2,4,5,3',4'-pentabromobiphenyl using the first method, but not the second. This decrease in activity was reversed by homogenizing the cells treated with 100 ng/ml pentabromobiphenyl. It is concluded that the direct homogenate assay of the enzyme may miss or underestimate decreases in its in vivo activity.