雅西卡（YASHICA）300Auto Focus单反相机

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计算机辅助教学（CAI）刍议

本文介绍了ＣＡＩ的基本原理、类型和特点，以及ＣＡＩ的历史概况，着重对我院ＣＡＩ工作的开展进行了分析研究。     

人类X染色体Xp21．3－11．3区YAC重叠群的构建

人类Ｘ染色体短臂２１．３—１１．３区是含有视网膜色素变性等数种遗传病基因位点的区域。我们对这个具有重要医学生物学意义的区段进行了ＹＡＣ重叠群构建。用这一区域已知的探针（ＯＴＣ、ＤＸＳ１６６、ＤＭＤｃＤＮＡ）及ＳＴＳ位标，以ＹＡＣ菌落原位杂交法及ＰＣＲ法进行了ＹＡＣ的筛选；也采用了法国ＣＥＰＨ和英国ＩＣＲＦ的部分ＹＡＣ；总共得到了５５个阳性ＹＡＣ。对上述ＹＡＣ进行了长度测定，２６对微卫星ＳＴＳ图谱分析，单拷贝探针的杂交定位，Ａｌｕ－ＰＣＲ指纹图谱分析。综合上述信息，对这些ＹＡＣ进行了排序，在Ｘｐ２１．３－１１．３区得到了６个０ＹＡＣ重叠群，覆盖了约１５Ｍｂ的范围。这些ＹＡＣ重叠群的构建为开展该区域疾病基因的定位克隆（Ｐｏｓｉｔｉｏｎａｌｃｌｏｎｉｎｇ）及ＤＮＡ顺序测定奠定了基础。     

铁路车辆电气设备设计中的CAD经验

作者论及引入和应用ＣＡＤ的重要步骤，如：ＣＡＤ系统的选择、ＣＡＤ应用的组织实施，操作人员的培训、以及软硬件的配置。列举了电路图的绘制和铁路车辆电气 三维方案设计应用实例，经验证明，在适应性和变型设计中应用ＣＡＤ，可以提高设计捏和柔性、缩短设计周期，并对ＣＡＤ应用中遇到的问题进行了。     

SiC-Al界面Al_4C_3的生成及其控制

系统研究了在Ａｌ中添加Ｓｉ对控制ＳｉＣ－Ａｌ之间生成Ａｌ４Ｃ３的化学反应的作用和对ＳｉＣ－Ａｌ系统化学反应动力学的影响，以及温度对化学反应程度的影响，探讨了Ａｌ４Ｃ３生成的机理。研究表明，添加Ｓｉ于Ａｌ中使ＳｉＣ和Ａｌ之间生成Ａｌ４Ｃ３的化学反应得到有效的控制并明显影响化学反应的速度；ＳｉＣ－Ａｌ系统化学反应的程度随温度升高而增大；Ａｌ４Ｃ３的生成通过两个步骤进行，即ＳｉＣ溶解于熔融金属Ａｌ中，然后和Ａｌ发生化学反应。研究结果为用熔融金属加工技术合成无Ａｌ４Ｃ３生成的ＳｉＣ／Ａｌ复合材料提供了可靠的途径。     

在振动磨中PVC的降解及与MMA共聚反应的研究

考察了温度、振幅、钢球直径等对ＰＶＣ在振动磨中降解的影响，确定ＰＶＣ力化学降解为无规断链过程。用力化学方法在振动磨中合成了ＭＭＡ－ＰＶＣ共聚物，通过ＩＲ和ＮＭＲ对ＭＭＡ－ＰＶＣ共聚物结构进行了鉴定，研究了ＰＶＣ／ＭＭＡ配比和振磨时间对共聚反应产率及共聚物组成的影响。热失重分析、ＳＥＭ观察和冲击强度测定结果表明，ＭＭＡ－ＰＶＣ共聚物比ＰＶＣ具有较高的热稳定性；ＭＭＡ－ＰＶＣ共聚物对ＰＶＣ／ＰＨＭＡ（聚甲基丙烯酸己酯）体系有增容作用     

Al＋Ti＋C复合系热爆反应合成过程及相组成研究EI

研究了Ａｌ含量和Ｃ／Ｔｉ对Ａｌ＋Ｔｉ＋Ｃ复合系热爆反应合成Ａｌ／ＴｉＣ的反应过程及生成相组成的影响。实验结果表明：随着Ａｌ含量的增加，反应温度降低，反应时间延长，但反应起始温度几乎没有变化；Ｃ／Ｔｉ对反应温度和反应时间有很大的影响，但对反应起始温度影响很小。在对生成相组成的研究中发现：当Ｃ／Ｔｉ＝１．２５、Ａｌ含量不大于６０ａｔ％和Ｃ／Ｔｉ＝１、Ａｌ含量不大于５０ａｔ％时，生成物只有ＴｉＣ；随着Ａｌ含量的增加，生成Ａｌ＿３Ｔｉ的量增加，并通过热力学理论对反应合成自由能进行了计算，计算结果与试验结果相吻合。另外，通过扫描电子显微镜（ＳＥＭ）对生成的ＴｉＣ的组织形貌进行了观察。结果表明：生成的ＴｉＣ尺寸均匀，约为０．３～０．８μｍ，大多数呈球状，部分为块状。     

颗粒类型对颗粒增强铝基复合材料性能的影响

本文对粉末冶金法制备的ＳｉＣ和ＴｉＣ颗粒增强铝基复合材料进行了研究。试验表明，在颗粒含量相同、尺寸相当的条件下，ＴｉＣ增强Ａｌ基复合材料的强度和模量均低于ＳｉＣ增强Ａｌ基复合材料，但其屈强比却明显高于ＳｉＣ增强Ａｌ基复合材料。高温长时间等温处理对ＴｉＣ颗粒增强纯Ａｌ复合材料的强度没有明显的影响。     

Al2O3—TiC—Co与Al2O3—TiC陶瓷冲蚀磨损行为的比较研究

通过特殊的化学处理方法，完成了对Ａｌ２Ｏ３及ＴｉＣ陶瓷粉末的钴包覆，将包覆后的两种粉安７０ｗｔ％Ａｌ２Ｏ３－Ｃｏ和３０ｗｔ％ＴｉＣ－Ｃｏ的比例混合烧结出硬度和韧性都较理想的Ａｌ２Ｏ３－ＴｉＣ－Ｃｏ（ＡＴＣ）精细陶瓷，通过ＳＥＭ观察研究其冲饥蚀磨损行为，并对ＡＴ３０（７０ｗｔ％Ａｌ２Ｏ３－３０ｗｔ％ＴｉＣ）和ＡＴＣ陶瓷的冲蚀行为机制进行了比较研究，与ＡＴ３０陶瓷相比，ＡＴＣ陶瓷良好的综合力学性能和细     

Microfluidic high-resolution free-flow isoelectric focusing

A microfluidic free-flow isoelectric focusing glass chip for separation of proteins is described. Free-flow isoelectric focusing is demonstrated with a set of fluorescent standards covering a wide range of isoelectric points from pH 3 to 10 as well as the protein HSA. With respect to an earlier developed device, an improved microfluidic FFE chip was developed. The improvements included the usage of multiple sheath flows and the introduction of preseparated ampholytes. Preseparated ampholytes are commonly used in large-scale conventional free-flow isoelectric focusing instruments but have not been used in micromachined devices yet. Furthermore, the channel depth was further decreased. These adaptations led to a higher separation resolution and peak capacity, which were not achieved with previously published free-flow isoelectric focusing chips. An almost linear pH gradient ranging from pH 2.5 to 11.5 between 1.2 and 2 mm wide was generated. Seven isoelectric focusing markers were successfully and clearly separated within a residence time of 2.5 s and an electrical field of 20 V mm-1. Experiments with pI markers proved that the device is fully capable of separating analytes with a minimum difference in isoelectric point of Delta(pI) = 0.4. Furthermore, the results indicate that even a better resolution can be achieved. The theoretical minimum difference in isoelectric point is Delta(pI) = 0.23 resulting in a peak capacity of 29 peaks within 1.8 mm. This is an 8-fold increase in peak capacity to previously published results. The focusing of pI markers led to an increase in concentration by factor 20 and higher. Further improvement in terms of resolution seems possible, for which we envisage that the influence of electroosmotic flow has to be further reduced. The performance of the microfluidic free-flow isoelectric focusing device will enable new applications, as this device might be used in clinical analysis where often low sample volumes are available and fast separation times are essential.     

Dynamic isoelectric focusing for proteomics

Dynamic isoelectric focusing is a new technique that is related to capillary isoelectric focusing but uses additional high-voltage power supplies to provide control over the shape of the electric field within the capillary. Manipulation of the electric field changes the pH gradient, enabling both the location and width of the focused protein bands to be controlled. The proteins can be migrated to a designated sampling point while remaining focused, where they can be collected for further analysis. This ability to collect and isolate the protein bands while maintaining a high peak capacity demonstrates that dynamic isoelectric focusing has great potential as a first dimension in a multidimensional separation system. Dynamic isoelectric focusing can achieve a peak capacity of over 1000, as shown by both mass spectrometry analysis and direct imaging.     

Fluorescence-labeled peptide pI markers for capillary isoelectric focusing

Nineteen fluorescent pH standards or pI markers ranging pH 3.64-10.12 were developed for use in capillary isoelectric focusing using laser-induced fluorescence detection. Tetra- to tridecapeptides containing one cysteine residue were designed to focus sharply at their respective isoelectric points by including amino acids that contain charged side chains, the pKa values of which are close to the corresponding pI values. An iodoacetylated derivative of tetramethylrhodamine was coupled to the thiol group of cysteine to yield fluorescent pI markers. The pI values of the labeled peptides were precisely determined after isoelectric focusing on polyacrylamide gel slabs by direct measurement of the pH of the focused bands. The markers were subjected to capillary isoelectric focusing for 10-15 min in coated capillaries under conditions of low electroosmosis and were detected by means of a scanning laser-induced fluorescence detector down to a level of subpicomolar range. The markers permitted the calibration of a wide-range pH gradient formed in a capillary by fluorescence detection for the first time and should facilitate the development of highly sensitive analytical methods based on a combination of capillary isoelectric focusing and laser-induced fluorescence detection.     

High-resolution capillary isoelectric focusing of complex protein mixtures from lysates of microorganisms

High-resolution capillary isoelectric focusing separations of complex protein mixtures have been obtained for cellular lysates of Saccharomyces cerevisiae, Eschericia coli, and Deinococcus radiodurans. High quality separations are shown to be achievable for total protein concentrations of < 0.1 mg/mL. The separation reproducibility was examined, and the influence of the capillary inner wall coating on resolution investigated using fusedsilica capillaries coated with various hydrophilic polymers including hydroxypropyl cellulose, poly(vinyl alcohol), and linear polyacrylamide. Proteins having an isoelectric point (pI) difference of 0.004 are shown to be separated using a linear carrier ampholyte (linear pH gradient between two electrodes) of 3-10. Approximately 45 discrete peaks in the pI range of 5-7 were obtained for S. cerevisiae, approximately 80 peaks in the pI range of 4.5-8.5 for E. coli, and approximately 210 peaks in the pI range of 3-8.8 for D. radiodurans.     

Capillary isoelectric focusing and fluorometric detection of proteins and microorganisms dynamically modified by poly(ethylene glycol) pyrenebutanoate

The nonionogenic pyrene-based tenside, poly(ethylene glycol) pyrenebutanoate, was prepared and applied in capillary isoelectric focusing with fluorometric detection. This dye was used here as a buffer additive in capillary isoelectric focusing for a dynamic modification of the sample of proteins and microorganisms. The values of the isoelectric points of the labeled bioanalytes were calculated with use of the fluorescent pI markers and were found comparable with pI of the native compounds. The mixed cultures of proteins and microorganisms, Escherichia coli CCM 3954, Staphylococcus epidermidis CCM 4418, Proteus vulgaris, Enterococcus faecalis CCM 4224, and Stenotrophomonas maltophilia, the strains of the yeast cells, Candida albicans CCM 8180, Candida krusei, Candida parapsilosis, Candida glabrata, Candida tropicalis, and Saccharomyces cerevisiae were reproducibly focused and separated by the suggested technique. Using UV excitation for the on-column fluorometric detection, the minimum detectable amount was down to 10 cells injected on the separation capillary.     

Concentration and separation of proteins in microfluidic channels on the basis of transverse IEF

The use of microfluidic channels formed by two electrodes made of gold or palladium to perform transverse isoelectric focusing (IEF) is presented as a means for continuous concentration and fractionation of proteins. The microchannels were 40 mm long with an electrode gap of 1.27 mm and a depth of 0.354 mm. The properties of pH gradients formed as a result of the electrolysis of water were influenced by variation of parameters such as the initial pH, ionic strength, and flow rate. Transverse IEF in pressure-driven flow is demonstrated using bovine serum albumin in a single ampholyte buffer as well as in multiple-component buffers. Experimental results of protein focusing compare well to predictions of a mathematical model. Optimal conditions for efficient continuous fractionation of a protein mixture are summarized and discussed.     

Proteome analysis of microdissected tumor tissue using a capillary isoelectric focusing-based multidimensional separation platform coupled with ESI-tandem MS

This study demonstrates the ability to perform sensitive proteome analysis on the limited protein quantities available through tissue microdissection. Capillary isoelectric focusing combined with nano-reversed-phase liquid chromatography in an automated and integrated platform not only provides systematic resolution of complex peptide mixtures based on their differences in isoelectric point and hydrophobicity but also eliminates peptide loss and analyte dilution. In comparison with strong cation exchange chromatography, the significant advantages of electrokinetic focusing-based separations include high resolving power, high concentration and narrow analyte bands, and effective usage of electrospray ionization-tandem MS toward peptide identifications. Through the use of capillary isoelectric focusing-based multidimensional peptide separations, a total of 6866 fully tryptic peptides were detected, leading to the identification of 1820 distinct proteins. Each distinct protein was identified by at least one distinct peptide sequence. These high mass accuracy and high-confidence identifications were generated from three proteome runs of a single glioblastoma multiforme tissue sample, each run consuming only 10 microg of total protein, an amount corresponding to 20,000 selectively isolated cells. Instead of performing multiple runs of multidimensional separations, the overall peak capacity can be greatly enhanced for mining deeper into tissue proteomics by increasing the number of CIEF fractions without an accompanying increase in sample consumption.     

Fully automated two-dimensional electrophoresis system for high-throughput protein analysis

We developed a fully automated electrophoresis system for rapid and highly reproducible protein analysis. All the two-dimensional (2D) electrophoresis procedures including isoelectric focusing (IEF), on-part protein staining, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and in situ protein detection were automatically completed. The system comprised Peltiert devices, high-voltage generating devices, electrodes, and three disposable polymethylmethacrylate (PMMA) parts for IEF, reaction chambers, and SDS-PAGE. Because of miniaturization of the IEF part, rapid IEF was achieved in 30 min. A gel with a tapered edge gel on the SDS-PAGE part realized a connection between the parts without use of a gluing material. A biaxial conveyer was employed for the part relocation, sample introduction, and washing processes to realize a low-maintenance and cost-effective automation system. Performances of the system and a commercial minigel system were compared in terms of detected number, resolution, and reproducibility of the protein spots. The system achieved high-resolution comparable to the minigel system despite shorter focusing time and smaller part dimensions. The resulting reproducibility was better or comparable to the performance of the minigel system. Complete 2D separation was achieved within 1.5 h. The system is practical, portable, and has automation capabilities.     

High-efficiency capillary isoelectric focusing of peptides

Several approaches are presently being developed for global proteome characterization that are based upon the analysis of polypeptide mixtures resulting from digestion of (often complex) mixtures of proteins. Improved methods for peptide analysis are needed that provide for sample concentration, higher resolution separations, and direct compatibility with mass spectrometry. In this work, methods for the high-efficiency capillary isoelectric focusing (CIEF) separation of peptides have been developed that provide for simultaneous sample concentration and separation according to peptide isoelectric point. Under typical nondenaturing CIEF conditions, peptides are concentrated approximately 500-fold, and peptides present at < 1 ng/ microL were detectable using conventional UV detection. CIEF separations of peptides provided much faster measurements of isoelectric points compared with conventional isoelectric focusing in gels. Very small differences in peptide isoelectric points (deltapI approximately 0.01) could be resolved, High-efficiency CIEF separations for complex peptide mixtures from tryptic digestion of yeast cytosol fractions were obtained and showed significant improvement over those obtained using capillary zone electrophoresis and packed capillary reversed-phase liquid chromatography.     

Separation of plant pathogens from different hosts and tissues by capillary electromigration techniques

In this contribution capillary isoelectric focusing and capillary zone electrophoresis were applied for the separation and detection of different plant pathogens including Pseudomonas syringae pv. syringae, P. syringae pv. lachrymans, Pseudomonas savastanoi pv. fraxinus, P. savastanoi pv. olea, Agrobacterium tumefaciens, A vitis, Xanthomonas arboricola pv. juglandis, X. campestris pv. zinniae, and Curtobacterium sp.. The UV detection and sensitive fluorescence detection of the native phytopathogens or those dynamically modified by the nonionogenic fluorescent tenside based on pyrenebutanoate were used. The isoelectric points of the labeled phytopathogens were found comparable with the pI of the native compounds. No influence of the hosts on pIs of the strains of the genus Pseudomonas was observed. The identification of plant pathogens by gas chromatographic analysis of fatty acid methyl esters was compared with results of capillary isoelectric focusing. Capillary electromigration was successfully applied for the separation of microbes directly from plant tissue suspensions.