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The subcellular distribution of the naturally occurring radionuclide 210 Po was investigated in the liver of the Atlantic mackerel Scomber scombrus, The majority of the 210 Po was found in the cytosol of the liver cells. Fractionation of the cytosol proteins by high performance size-exclusion and ion-exchange chromatography indicated that about 30% of 210 Po was bound to ferritin and approximately 28% to metallothioneins. The affinity of 210 Po for these proteins was confirmed by a similar binding of the artificial 208 Po isotope incubated in vitro with the cytosolic proteins. Two other proteins, likely selenium- and zinc-containing enzymes, may also bind smaller amounts of 210 Po, about 8 % each. The extensive binding of 210 Po to ferritin and metallothioneins is not accompanied by a similar strong binding of 210 Pb, the radioactive grandparent of 210 Po, which explains the generally very high 210 Po: 210 Pb ratio observed in fish tissues and, in particular, fish liver.

210Po binding to metallothioneins and ferritin in the liver of teleost marine fish