Cu~+、Ag~+、Au~+与乙硫醇的气相化学反应

利用激光溅射 分子束的技术 ,结合反射飞行时间质谱计 ,研究了Cu+、Ag+、Au+与乙硫醇的气相化学反应。结果显示这三种金属离子与 (CH3 CH2 SH) n 反应形成一系列团簇离子M+(CH3 CH2 SH) n,且团簇离子尺寸不一样。Ag+、Au+与乙硫醇的反应还生成了 (CH3 CH2 SH) +n ,由此推测Cu+、Ag+、Au+与乙硫醇团簇的反应存在两种通道 ,一种通道是生成M+(CH3 CH2 SH) n,另一种是生成 (CH3 CH2 SH) +n 。Cu+、Au+与乙硫醇的反应还生成了M+(H2 S) (M =Cu、Au) ,但是实验中没有观察到Ag+(H2 S) ,理论计算表明Ag+(H2 S)很不稳定。另外 ,分析产物离子M+(CH3 CH2 SH) n 的强度发现 ,n =1～ 2之间存在明显的强度突变现象     

激光沉积超导薄膜过程中出射粒子速度的飞行时间谱分析

采用飞行时间谱技术,测量了准分子激光烧蚀沉积高温超导薄膜过程中,由靶面出射粒子的飞行速度。研究了粒子速度与充氧压及其激光能量密度的关系。讨论了高能粒子在薄膜原位低温外延生长中的作用。     

钒氧阴离子团簇与小分子碳氢化合物反应的实验和理论研究

为了在分子层次上揭示相关催化反应的机理, 人们对过渡金属氧化物团簇与碳氢化合物分子反应进行了大量研究. 相比于过渡金属氧化物团簇阳离子, 阴离子对一些碳氢化合物的活性弱得多, 因此研究还很少. 在本工作中, 我们通过激光溅射产生钒氧团簇阴离子VxOy, 产生的团簇在接近热碰撞条件下与烷烃(C2H6和C4H10)以及烯烃(C2H4和C3H6) 在一个快速流动反应管中进行反应, 飞行时间质谱用来检测反应前后的团簇分布. 在VxOy与烷烃的反应中, 生成了产物V2O6H-和V4O11H-; 在与烯烃的反应中, 产生了相应的吸附产物V4O11X-(X=C2H4或C3H6). 密度泛函理论计算表明: V2O-6和V4O-11可以活化烷烃(C2H6和C4H10)的C—H键, 也可以与烯烃(C2H4和C3H6)发生3+2环化加成反应形成一个五元环结构(-V-O-C-C-O-), C—H键活化与环加成反应都需经历可以克服的反应能垒. 理论计算与实验观测结果相符合. V2O-6和V4O-11团簇都具有氧原子自由基(O·或O-)的成键特征, 活性O-物种也经常出现在钒氧催化剂表面, 因而本研究在分子水平上, 揭示了表面活性氧物种与碳氢化合物反应的机理.     

液相色谱/大气压化学电离飞行时间质谱分析氢化可的松中微量杂质

采用液相色谱/大气压化学电离飞行时间质谱测定氢化可的松对照品中微量杂 质，并采用源内碰撞诱导解离质谱进行了结构定性分析。方法简单，可靠，重现性 好。     

Protein secondary structure and stability determined by combining exoproteolysis and matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

In the post-genomic era, several projects focused on the massive experimental resolution of the three-dimensional structures of all the proteins of different organisms have been initiated. Simultaneously, significant progress has been made in the ab initio prediction of protein three-dimensional structure. One of the keys to the success of such a prediction is the use of local information (i.e. secondary structure). Here we describe a new limited proteolysis methodology, based on the use of unspecific exoproteases coupled with matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS), to map quickly secondary structure elements of a protein from both ends, the N- and C-termini. We show that the proteolytic patterns (mass spectra series) obtained can be interpreted in the light of the conformation and local stability of the analyzed proteins, a direct correlation being observed between the predicted and the experimentally derived protein secondary structure. Further, this methodology can be easily applied to check rapidly the folding state of a protein and characterize mutational effects on protein conformation and stability. Moreover, given global stability information, this methodology allows one to locate the protein regions of increased or decreased conformational stability. All of this can be done with a small fraction of the amount of protein required by most of the other methods for conformational analysis. Thus limited exoproteolysis, together with MALDI-TOF MS, can be a useful tool to achieve quickly the elucidation of protein structure and stability.     

钒氧阴离子团簇与小分子碳氢化合物反应的实验和理论研究

为了在分子层次上揭示相关催化反应的机理, 人们对过渡金属氧化物团簇与碳氢化合物分子反应进行了大量研究. 相比于过渡金属氧化物团簇阳离子, 阴离子对一些碳氢化合物的活性弱得多, 因此研究还很少. 在本工作中, 我们通过激光溅射产生钒氧团簇阴离子VxOy, 产生的团簇在接近热碰撞条件下与烷烃(C2H6和C4H10)以及烯烃(C2H4和C3H6) 在一个快速流动反应管中进行反应, 飞行时间质谱用来检测反应前后的团簇分布. 在VxOy与烷烃的反应中, 生成了产物V2O6H-和V4O11H-; 在与烯烃的反应中, 产生了相应的吸附产物V4O11X-(X=C2H4或C3H6). 密度泛函理论计算表明: V2O-6和V4O-11可以活化烷烃(C2H6和C4H10)的C—H键, 也可以与烯烃(C2H4和C3H6)发生3+2环化加成反应形成一个五元环结构(-V-O-C-C-O-), C—H键活化与环加成反应都需经历可以克服的反应能垒. 理论计算与实验观测结果相符合. V2O-6和V4O-11团簇都具有氧原子自由基(O·或O-)的成键特征, 活性O-物种也经常出现在钒氧催化剂表面, 因而本研究在分子水平上, 揭示了表面活性氧物种与碳氢化合物反应的机理.     

Multi-turn time-of-flight mass spectrometers with electrostatic sectors

The mass resolution of a time-of-flight (TOF) mass spectrometer is directly proportional to its total flight pathlength. Multi-turn or multi-passage ion optical geometries are necessary to obtain fight distances of sufficient length within reasonable size limitations. We have investigated ion optics for a multi-turn TOF mass spectrometer with electrostatic sectors. The concept of 'perfect' focusing conditions is introduced. Furthermore, a new type of multi-turn TOF mass spectrometer, the MULTUM Linear plus, was developed. It consists of four cylindrical electric sectors and 28 electric quadrupole lenses. It has a vacuum chamber 60 x 70 x 20 cm in size. Mass resolution is demonstrated to increase according to the number of ion cycles. A mass resolution of 350 000 (m/z = 28, FWHM) was achieved after 501.5 cycles. The MULTUM Linear plus analyzer is not simple, however; 28 electric quadrupole lenses are used. In order to reduce the number of ion optical parts, an improved multi-turn TOF mass spectrometer, the MULTUM II, consisting of only four toroidal electric sectors, was also developed. The possibility of tandem mass spectrometric applications using multi-turn TOF mass spectrometers is also discussed.     

Direct targeting of human plasma for matrix-assisted laser desorption/ionization and analysis of plasma proteins by time of flight-mass spectrometry

A method to analyze human plasma proteins without fractionation, directly applying a plasma-matrix mixture on the target plate of a matrix-assisted laser desorption/ionization-time of flight-mass spectrometer (MALDI-TOF-MS), has been described. Peaks of ionized plasma proteins could not be detected applying a mixture of an undiluted plasma sample and a matrix solution, but they appeared when the plasma was diluted before mixing with the matrix. Tenfold diluted plasma provided well-resolved protein peaks in the m/z range from 4000 to 30,000. The addition of a simple post-crystallization washing procedure performed on the target plate further improved the quality of mass spectra. We numbered 58 peaks in the range of 4-160 kDa and 32 out of which were assigned to the plasma protein species which have been reported. Especially high sensitivity and resolution were obtained in the region < 30 kDa, where multiple isoforms of apolipoprotein A-I, apolipoprotein A-II, apolipoprotein C-I, apolipoprotein C-II, apolipoprotein C-III, and transthyretin could be assigned. Various post-translational modifications are involved in the isoforms, e.g., proteolytic cleavage, glycosylation and chemical modifications. This method will become complementary with the present electrophoretic techniques, especially for the analysis of low-molecular-mass proteins.     

Fast simultaneous determination of 23 veterinary drug residues in fish,poultry, and red meat by liquid chromatography/tandem mass spectrometry

The misuses of veterinary drugs can result in the accumulation of residues in food of animal origin that can make its way to the final consumer. Herein we describe a simple method for the accurate determination of beta-lactams, quinolones, sulphonamides, and tetracyclines in fish, poultry, and red meat. No extraction cartridges were used; instead, the extraction process consisted of the addition of an organic solvents, shaking, centrifugation, and dilution. An extensive validation process demonstrated an excellent linearity (R² ≥ 0.99) for 23-drug residues. The recovery of drugs in different matrices at two concentration levels (n = 6) was in the range of 82–119%. The method was proved to be repeatable and reproducible with intra/inter-day measurements (RSDs lower than 20%). The quantification limits of drug residues were in the range of 0.8 to 45.3 ug/kg, which is well below the maximum residue limits set by most regulatory authorities. This method was successfully applied to the routine analysis of 20 fish, poultry, and red meat samples (n = 60).     

Identification of formylglycine in sulfatases by matrix-assisted laser desorption/ionization time-of-flight mass spectrometry

C(alpha)-Formylglycine, the catalytic amino acid residue in the active site of sulfatases, is generated by post-translational modification of a cysteine or serine residue. We describe a highly sensitive procedure for the detection of C(alpha)-formylglycine-containing peptides in tryptic digests of sulfatase proteins. The protocol is based on the formation of hydrazone derivatives of C(alpha)-formylglycine-containing peptides when using dinitrophenylhydrazine as a matrix for matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOFMS). The hydrazone derivatives desorb and ionize with high efficiency and can be detected in the sub-femtomole range. The presence of C(alpha)-formylglycine is indicated by a mass increment of 180.13 u, corresponding to the hydrazone moiety, and also by a unique C-terminal fragment ion, characteristic of sulfatases, that becomes prominent in MALDI post-source decay mass spectra of the hydrazone derivatives.