The present study reports the isolation and partial characterization of a lead-binding protein (PbBP) in the liver of the channel catfish (Ictalurus punctatus). The protein has a molecular weight of 10 kDa as determined by SDS polyacrylamide gel electrophoresis and contains relatively large amounts of glycine (18.3%), aspartic acid (10.2%) and serine (15.1%). Western blot studies conducted using polyclonal antibodies to the rat renal PbBP and metallothionein (MT) showed no cross-reactivity, suggesting that the fish hepatic protein is immunologically distinct from these low-molecular weight metal-binding proteins in mammals. © 1994.
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