Depuration of cadmium from Chlamys farreri by ZnSO4, EDTA-Na2 and sodium citrate in short time.

In view of high content of cadmium (Cd) in Chlamys farreri, a commercial edible shellfish species, depurating Cd from Chlamys farreri is an important topic nowadays, especially in short time. Therefore, three kinds of additives were introduced into seawater respectively, i.e. ZnSO4, EDTA-Na2, sodium citrate, to depurate Cd from Chlamys farreri. The alteration of Cd content in separate organs was investigated under several treatments with high depuration efficiency. The results showed that Cd was depurated exceeding 20% within 12 h by the combination of 0.15 g/L sodium citrate, 0.28 g/L ZnSO4, and 0.42 g/L EDTA-Na2. No obvious increase of Cd was observed in the adductor muscles, while Cd decreased in the other part, so the reduction of Cd in the whole organism of Chlamys farreri may occur. Cd reduction was found in the following organs: the digestive gland, kidney, gill, and mantle. Furthermore, Cd migration to gonad from other tissues was noticed.

Structural and binding studies of phosphopantetheine adenylyl transferase from Acinetobacter baumannii.

Phosphopantetheine adenylyltransferase (PPAT, EC. 2.7.7.3) catalyzes an essential step in the reaction that transfers an adenylyl group from adenosine tri phosphate (ATP) to 4'-phosphopantetheine (pPant) yielding 3'- dephospho-coenzyme A (dPCoA) and pyrophosphate (PP) in the coenzyme A (CoA) biosynthesis pathway. The enzyme PPAT from Acinetobacter baumannii (AbPPAT) was cloned, expressed and purified. The binding studies of AbPPAT were carried out with two compounds, tri­sodium citrate (TSC) and l-ascorbic acid (LAA, vitamin-C) using fluorescence spectroscopic (FS) and surface Plasmon resonance (SPR) methods. Both methods provided similar values of dissociation constants for TSC and LAA which were of the order of 10-8 M and 10-5 M respectively. The computer aided docking studies indicated fewer interactions of LAA with AbPPAT as compared to those of TSC. The freshly purified samples of AbPPAT were crystallized. The crystals of AbPPAT were soaked in the solutions containing TSC and LAA. However, the crystals of the complex of AbPPAT with LAA did not diffract well and hence the structure of the complex of AbPPAT with LAA could not be determined. On the other hand, the crystals of the complex of AbPPAT with TSC diffracted well and the structure was determined at 1.76 Šresolution. It showed that TSC bound to AbPPAT at the ATP binding site and formed several intermolecular contacts including 12 hydrogen bonds. The results of binding studies for both TSC and LAA and the structure of the complex of AbPPAT with TSC clearly indicated a potential role of TSC and LAA as antibacterial agents.