Beijing Mass Spectrometry Center
Beijing Mass Spectrometry Center
Zhen C.,CAS Institute of Chemistry |
Zhen C.,CAS Beijing National Laboratory for Molecular |
Zhou Y.,CAS Institute of Chemistry |
Zhou Y.,CAS Beijing National Laboratory for Molecular |
And 11 more authors.
Analyst | Year: 2013
Chinese liquors are often a very important part of social event in China. Driven by high profit, some illegal traders often use inferior liquors instead of the products with high quality to cheat the customer. Therefore, it is highly required to authenticate Chinese liquors. In this paper a novel method based on ambient glow discharge ionization mass spectrometry has been developed to differentiate Chinese liquors. Volatile components from liquor samples were ionized by the plasma generated by glow discharge and then detected by a commercial linear ion trap mass spectrometer. Consequently, the fingerprint mass spectra of several Chinese liquors were obtained. Combined with principal component analysis, this new method was successfully applied to differentiate different brands of Chinese liquors without any sample pretreatment. Compared with conventional methods, this novel method has the advantages of easy operation, high speed, and high efficiency, which make it a potential tool in the fields of food safety, atmosphere chemistry.© 2013 The Royal Society of Chemistry.
Ma L.,CAS Institute of Chemistry |
Xin B.,Beijing Mass Spectrometry Center |
Chen Y.,CAS Institute of Chemistry |
Chen Y.,CAS Beijing National Laboratory for Molecular |
Chen Y.,Beijing Mass Spectrometry Center
Analyst | Year: 2012
The detection of explosives in soil is of great significance in public security programmes and environmental science. In the present work, a ppb-level method was established to directly detect the semi-volatile explosives, RDX and TNT, present in complex soil samples. The method used thermal sampling technique and a direct current atmospheric pressure glow discharge source mounted with a brass cylinder electrode (9 mm × 4.6 mm i.d./5.6 mm o.d.) to face the samples, requiring no sample pretreatment steps such as soil extraction (about ten hours). It was characterized by the merits of easy operation, high sensitivity and fast speed, and has been validated by real soil samples from various locations around a factory or firecracker releasing fields. It took only 5 min per sample, with the limit of detection down to 0.5 ppb (S/N = 3) trinitrohexahydro-1,3,5-triazine in soils heated at 170 °C. It is also extendable to the analysis of other volatile analytes. © The Royal Society of Chemistry 2012.
Lin Y.,CAS Beijing National Laboratory for Molecular |
Lin Y.,CAS Institute of Chemistry |
Huang Y.,CAS Institute of Process Engineering |
Zheng W.,CAS Beijing National Laboratory for Molecular |
And 13 more authors.
Journal of Inorganic Biochemistry | Year: 2015
Abstract Electrospray ionization mass spectrometry (ESI-MS) has been widely used to identify binding sites of metal complexes to proteins. However, the MS quantification of the metal-protein coordination remains a challenge. We have recently demonstrated by ESI-MS analysis that organometallic ruthenium complexes [(η6-arene)Ru(en)Cl]+ (arene = p-cymene (1), biphenyl (2) or 9,10-dihydrophenanthrene (3); en = ethylenediamine) bound to human glutathione-S-transferase π (GSTπ) at Cys15 and Cys48 within the G-site, and Cys102 and Met92 on the interface of the GSTπ dimer, showing inhibitory potency against the enzyme (J. Inorg. Biochem., 128 (2013) 77-84). Herein, we developed a mass spectrometric method to quantify the binding stoichiometry of the three complexes to GSTπ. The differences in signal intensities of the heavy-labelled peptides produced by tryptic digestion of the ruthenated GSTπ complexes and the respective light-labelled peptides in the tryptic digest of equimolar GSTπ were used to calculate the binding stoichiometry at specific residues. The results indicated that the pre-complexation of GSTπ with its substrate GSH significantly reduced the bindings of the ruthenium complexes at Met92 and Cys102, but had little impact on the bindings at Cys15 and Cys48. As the inhibitory activities of the ruthenium complexes against GSTπ are similar to those against GSTπ in complexation with GSH, these results suggest that the inhibition of the ruthenium complexes on GSTπ is attributed to the ruthenation at Cys15 and Cys48. The present work provides not only insights into the understanding on the inhibitory mechanism of ruthenium complexes GSTπ, but also a general method for quantitative characterization of metal-protein interactions. © 2015 Elsevier Inc. All rights reserved.