Preconcentration of mercury using duolite GT-73 in the analysis of water samples by inductively coupled plasma atomic emission spectrometry.

Duolite GT-73 resin was used for the preconcentration of Hg(II) from hydrochloric acid media as well as separation of the analyte from diversity of the co-existing metal ions (Al, Ca, Cd, Co, Cr, Cu, Fe, Mg, Mn, Ni, Pb and Zn) in off-line column operation. Due to the high affinity of the resin to the transition metals, Hg was adsorbed alongside with the foreign metals investigated. A complete release of the concomitant metals from the resin without the desorption of Hg was carried out using solutions of HCl and HNO3. A quantitative recovery of Hg was obtained by digestion of the resin using a H2SO4 and H2O2 mixture in an open-vessel system. An enrichment factor of 40 was achieved. The devised procedure was applied for the determination of Hg(II) in tap-water samples.     

Kupfer

Analytical and Bioanalytical Chemistry -     

Die colorimetrische Bestimmung der Platinmetalle mit Nitroso-R-Salz

Ohne Zusammenfassung     

Crystal Structure and Packing of Isocyclosporin A

The crystal structure of isocyclosporin A ( 1 ), a rearrangement product of the immunosuppressant drug cyclosporin A, has been determined at 193 (2) K. Crystals are orthorhombic with cell dimensions a = 26.684 (7), b = 26.936 (3) Å, c = 28.549 (7) Å, space group C222₁. The structure was solved by direct methods and refined by full-matrix least-squares methods to a conventional R value of 0.110. In contrast to the structure of cyclosprin A in solution and in the crystal, isocyclosporin A ( 1 ) has no regular secondary structural elements. The backbone adopts an open, irregular conformation with cis amide bonds between residue 2 and 3, and 3 and 4, respectively. All the other amide bonds and the ester linkage are trans. Contrary to crystal structures of cyclosporin derivatives, this crystal structure is stabilized by two transannular and four intermolecular H-bonds.     

Die Kristallstruktur von AlI3 2 Pl3: ein P2I5+ AlI4−

Crystal Structure of AlI₃ · 2 PI₃:P₂I₅⁺ AlI₄^? The crystal structure of the title compound was determined from single crystal X-ray data. P₂I₅⁺AlI₄^? crystallizes in the orthorhombic space group Pbca, a = 1 088.3, b = 1 827.3, c = 2 031.6 pm, V = 4040 · 10⁶ pm³, Z = 8. The P₂I₅⁺ and AlI₄^? ions are connected by weak iodine-iodine bonds (I? I distances between 343.5 and 376.3 pm). The mean P? I and Al? I bond lengths were found to be 240.9 and 252.9 pm respectively.     

The Molecular and Crystal Structure of the Glycopeptide A-40926 Aglycone

The crystal structure of a glycopeptide antibiotic A–40926 aglycone was investigated by X-ray analysis at ?120°. A-40926 crystallises in the orthorhombic space group P2₁2₁2₁ with two monomers in the asymmetric unit, a = 21.774(4), b = 28.603(7), c = 29.757(4) Å. ‘Conventional’ direct methods approach failed to solve the structure, but a novel iterative real/reciprocal space procedure was successful. Refinement against 11248 F² data led to R1 = 13.3% for 6770 F > 4σ (F). The two monomers of A-40926 have similar conformations and are bound by antiparallel H-bonds to form a ‘chain’ structure of connecting dimers. The antibiotic molecule possesses a ‘binding pocket’ for the C-terminal carboxy group of the cell-wall protein, which is consisten with suggestions based on NMR data and the recently reported crystal structure of ureido-balhimycin. In A-40926 the monomers are polymerically linked by H-bonds, quite unlike the tight dimer formation observed in ureido-balhimycin.