Determination of tungsten and insoluble compounds in the air of workplace by ICP-OES / 中华劳动卫生职业病杂志

Objective@#To establish the method for determination of tungsten and insoluble compounds in the air of workplace by inductively coupled plasma optical emission spectrometry (ICP-OES) .@*Methods@#The tungsten and insoluble compounds were digested by microwave digestion apparatus using nitric acid and hydrofluoric acid, detected by ICP-OES.@*Results@#The linearity of tungsten and insoluble compounds (as tungsten) were good at the range of 0.16-100.0 μg/ml, the minimum quantitation concentration was 0.11 mg/m3, the recovery was ranged from 81.9%-97.1%, the RSD of intra-and inter-batch precision were 0.5%-2.5% and 1.2%-4.4%, respectively.@*Conclusion@#The determination method meet the requirement of analysis and apply to the determination of tungsten and insoluble compounds in the air of workplace.

Structural basis for inhibition of protein tyrosine phosphatases by Keggin compounds phosphomolybdate and phosphotungstate

Protein-tyrosine phosphatases (PTPs) constitute a family of receptor-like, and cytoplasmic enzymes, which catalyze the dephosphorylation of phosphotyrosine residues in a variety of receptors and signaling molecules. Together with protein tyrosine kinases (PTKs), PTPs are critically involved in regulating many cellular signaling processes. In this study, diverse compounds were screened for PTP inhibition and selectively screened for inhibitors with the end product inhibition properties. Among phosphate analogues and their derivatives for PTP inhibition, Keggin compounds phosphomolybdate (PM) and phosphotungstate (PT) strongly inhibited both PTP-1B and SHP-1, with K(i) values of 0.06-1.2 micromM in the presence of EDTA. Unlike the vanadium compounds, inhibition potencies of PM and PT were not significantly affected by EDTA. PM and PT were potent, competitive inhibitors for PTPs, but relatively poor inhibitors of Ser/Thr phosphatase. Interestingly, PM and PT did not inhibit alkaline phosphatase at all. The crystal structure of PTP-1B in complex with PM, at 2.0 A resolution, reveals that MoO(3), derived from PM by hydrolysis, binds at the active site. The molybdenium atom of the inhibitor is coordinated with six ligands: three oxo-ligands, two apical water molecules and a S atom of the catalytic cysteine residue. In support of the crystallographic finding, we observed that molybdenium oxides (MoO(3), MoO(2), and MoO(2)Cl(2)) inhibited PTP-1B with IC(50) in the range 5-15 micromM.