Metal-binding proteins were investigated in livers of bream caught in
the River Elbe from Steti (Czech Republic) to Hamburg (Federal Republi
c of Germany). A major zinc and copper binding protein fraction with a
low molecular weight of 10 000 to 12 000 Da and with properties simil
ar to mammalian hepatic metallothionein was isolated from bream livers
using gel filtration chromatography. Two protein isoforms could be se
parated by reversed phase-high performance liquid chromatography (RP-H
PLC), however, mercury was associated with only one isoform. The possi
bility of different detoxification potentials of the isoforms is discu
ssed. Maximal concentrations of metal-binding protein were detected in
samples from Dresden. If metal-binding proteins are to be included in
a biological monitoring study, further investigations are required.