The teleost warm temperature acclimation related 65 kDa protein (Wap65) is a plasma glycoprotein with the potential roles in heat adaptation, heme recycling, immune response and copper metabolism. It is most homologous to the mammalian hemopexin, which is the plasma transporter of heme. A full-length cDNA clone of the Wap65 gene, 1,534 bp in size, was isolated from the fish ayu (Plecoglossus altivelis). Its deduced amino acid sequence of 439 residues had 60.4-65.4% and 38.3-47.3% identical to fish Wap65-2-type and Wap65-1-type sequences, respectively. In phylogenetic analysis, aWap65 grouped tightly with those fish Wap65-2-type sequences. In healthy control fish, the highest mRNA signal for aWap65 was from the liver, moderately high in brain and gill, and but weaker in spleen, kidney, muscle, heart and intestine. In Listonella anguillarum-infected fish, aWap65 transcripts were significantly increased in liver, while no obvious changes in other tissues at 12 hpi. However, aWap65 transcripts were significantly increased in various tissues at 24 hpi when hemolysis developing, suggesting that aWap65 might be involved in the immune response of ayu.

No abstract

No abstract

No abstract

Adsorption behavior of the iron impregnated, weakly basic resin D301 (Fe-D301) for removal of 2-naphthalenesulfonic acid (2-NSA) from aqueous solution was studied by using a fixed-bed column. The effects of process variables such as bed height, flow rate, and coexisting ions were investigated. The results indicated that the breakpoint and exhaustion point increased with increasing bed height and decreased with increasing 2-NSA flowrate. Experimental data showed a strong fit to the Bed Depth Service Time model. The coexisting ions in the 2-NSA solution had a clear effect on the breakthrough volume. The high extent of recovery of 2-NSA with good reproducibility provided an effective method for the separation of 2-NSA by the adsorbent Fe-D301.