A high-affinity zinc-binding plasma protein in channel catfish (Ictalurus punctatus).
1. Channel catfish (Ictalurus punctatus) have a remarkably high concentration of zinc (Zn) in their blood serum, about 20 micrograms/ml. However, compared to mammals, the concentrations of Zn in their tissues are not remarkable. The serum Zn is dialyzable against a solution containing 1 mM EDTA. 2. Following separation of serum proteins by gel-filtration most of the Zn was recovered in a fraction with the same peak volume of elution for the Zn and protein concentrations and having a molecular weight similar to bovine serum albumin. 3. Binding of Zn to such sites was not changed by Cu2+, Cd2+, Ca2+, or La3+. N-ethylemaleimide (NEM) appeared to decrease binding slightly. 4. Equilibrium dialysis with a Scatchard plot analysis of these data suggested that a single set of binding sites was present on the protein(s) with KD of 2 x 10(-5) M. There were binding sites for 35 x 10(-8) M Zn/mg protein. 5. Parallel equilibrium dialysis measurements using human, rabbit and chicken albumins indicated that the catfish serum protein(s) had a much higher affinity and binding capacity for Zn than the albumins in these species. 6. The catfish Zn serum-binding protein may be an albumin. The possible physiological significance of such a serum protein in freshwater fish is discussed.
Department of Anatomy, Physiological Sciences and Radiology, College of Veterinary Medicine, North Carolina State University, Raleigh 27606.
P J
PJ
Bentley
D000818:Animals; D001798:Blood Proteins / Q000378:metabolism*; D005033:Ethylmaleimide / Q000494:pharmacology; D007059:Ictaluridae / Q000378:metabolism*; D011485:Protein Binding; D015032:Zinc / Q000378:metabolism*
D001798:Blood Proteins; D015032:Zinc; D005033:Ethylmaleimide