125I粒子条联合胆道支架植入治疗恶性梗阻性黄疸22例疗效分析

【摘要】　 　目的 研究和探讨125I粒子条联合胆道支架植入治疗恶性梗阻性黄疸的临床疗效。方法 2011年6月—2013年9月收治恶性梗阻性黄疸患者40例。行胆道支架植入术治疗患者18例，为对照组；采用125I粒子条联合胆道支架植入患者22例，为观察组。两组均采用经皮肝穿刺胆道引流（PTCD）并胆道支架植入。结果 观察组与对照组的平均胆道开通时间分别为（8.7 ± 0.7）和（6.2 ± 0.4）个月，两组比较差异有统计学意义（P < 0.05）。观察组与对照组术后平均生存时间分别为（11.4 ± 0.8）和（8.7 ± 0.5）个月，生存时间的差异有统计学意义（P < 0.05）。术后近期疗效及并发症两组之间的比较无明显差异（P > 0.05），但是远期疗效有显著差异（P < 0.05）。结论 与对照组相比，观察组的术后生存时间及胆道开通时间明显延长，对于125I粒子条联合支架治疗恶性梗阻性黄疸值得进一步临床研究。
     

Na+、K+离子交换对Co-Mo/MCM-41加氢脱硫催化剂的影响

 用偏硅酸钠和正硅酸乙酯作硅源制备了MCM-41（分别记作MCM-41(S)和MCM-41(T)）分子筛，并用Na₂C₂O₄和K₂C₂O₄对MCM-41(S)进行了碱金属离子交换改性。以质量分数0.8 %的二苯并噻吩（DBT）的十氢萘溶液为模型化合物，考察了不同MCM-41担载的Co-Mo硫化物催化剂对DBT的加氢脱硫反应性能。结果表明，MCM-41担载的Co-Mo催化剂加氢活性较低，DBT主要通过直接脱硫反应路径脱硫。其活性顺序为：Co-Mo/MCM-41(T)>Co-Mo/MCM-41(S)>Co-Mo/MCM-41(K)>Co-Mo/MCM-41(Na)。UV-Vis结果表明，部分Co与MCM-41(S)中少量Al发生相互作用，生成了CoAl₂O₄，是造成Co-Mo/MCM-41(S)活性降低的重要因素。而在Co-Mo/MCM-41(K)和Co-Mo/MCM-41(Na)中，除CoAl₂O₄物种之外，碱金属的引入还促进了Co₃O₄物种的形成，使其活性进一步降低。     

一种PD雷达动目标模拟与微波测控系统

介绍了一种基于PC／104总线，具有GPIB程控功能，采用无内部微波源体制，通过在雷达载频上调制多普勒频率模型目标速度信息，延迟雷达发射机触发脉冲模拟目标距离信息并具有微波功率精确定标与衰减功能的PD雷达动目标模拟与微波测控系统。     

Breaking a remote user authentication scheme for multi-server architecture

Lin et al., (2003) proposed a remote user authentication scheme for multi-server architecture. In this paper, we breaks this scheme by giving an attack. Our attack allows an adversary to impersonate any user in the system, as long as a single authentication message of that user is observed.     

一种微透镜阵列的研制

介绍一种利用表面张力的作用、以光纤作材料、用分离的自聚焦透镜制作微透镜阵型的方法，这种方法具有制作工艺简单、无须昂贵设备等优点，用此方法实际制作了具有良好连续面型的微透镜阵列，并对制作的微透镜阵列进行了测试，效果较好。     

激光熔覆专用铁基合金粉末的研究进展

指出了目前防止熔覆层开裂所采取的主要措施中存在的问题,阐述了激光熔覆和热喷涂对于所用合金粉末性能要求之异同,评述了激光熔覆专用铁基合金粉末的研制现状,提出了成分与组织设计的新思想。     

A noncompetitive peptide inhibitor of the nicotinic acetylcholine receptor from Conus purpurascens venom

A paralytic peptide, psi-conotoxin Piiie has been purified and characterized from Conus purpurascens venom. Electrophysiological studies indicate that the peptide inhibits the nicotinic acetylcholine receptor (nAChR). However, the peptide does not block the binding of alpha-bungarotoxin, a competitive nAChR antagonist. Thus, psi-conotoxin Piiie appears to inhibit the receptor at a site other than the acetylcholine-binding site. As ascertained by sequence analysis, mass spectrometry, and chemical synthesis, the peptide has the following covalent structure: HOOCCLYGKCRRYOGCSSASCCQR* (O = 4-trans hydroxyproline; * indicates an amidated C-terminus). The disulfide connectivity of the toxin is unrelated to the alpha- or the alphaA-conotoxins, the Conus peptide families that are competitive inhibitors of the nAChR, but shows homology to the mu-conotoxins (which are Na+ channel blockers).     

A magnetic resonance imaging study of planum temporale asymmetry in men with developmental dyslexia

The influence of ionic strength and composition on the binding and inhibition of human leukocyte elastase by glycosaminoglycans with variable degree and position of sulfation was investigated. The kinetic mechanism of inhibition had a hyperbolic, mixed-type character with a competitive component that was promoted by low ionic strength, reduced by phosphate ions, and which also depended on the substrate and glycosaminoglycan structure. Enzyme binding was a cooperative phenomenon that varied with ionic strength and composition. The inhibition patterns correlated with the cationic character of elastase and with the distribution of arginines on its molecular surface, most notably with residues located in the vicinity of the substrate binding region. The order of affinity for elastase binding was chondroitin 4-sulfate < chondroitin 6-sulfate < dermatan sulfate, iduronate-containing derivatives being superior with respect to the glucuronate-containing counterparts. Additional sulfation at both the 4- and 6- positions or at the N- and 4-positions of the N-acetylgalactosamine moiety decidedly improved the inhibitory efficiency. The results highlight a fundamental physiological role of enzyme-glycosaminoglycan interactions. In the azurophil granule of the human polymorphonuclear neutrophil, elastase and other enzymes are bound to a matrix of chondroitin 4-sulfate because this is the only glycosaminoglycan that simultaneously offers good binding for enzyme compartmentalization together with prompt release from the bound state at the onset of phagocytosis.