渐变折射率波导传播特性微扰计算的代数递推公式

应用量子力学的超位力定理（HVT）和赫尔曼－费恩曼（Hellmann-Feynman）定理（HFT），导出了用微扰法计算渐变折射率平面波导传播常数各级近似值的代数递推公式，并给出了由传播常数近似值计算模场近似表达式的代数式。计算了几个典型实例，此法的特点是便于直接计算任意级近似的传播常数及模场分布，且可推广到二维波导的计算。     

双轴晶体电光调制器的最优设计

运用新的线性电光效应的耦合波理论，对双轴晶体KTP电光调制器的温度特性进行了理论研究.找到了一个入射光波矢的方向，在该方向上，出射光光强不随温度的变化而变化，而且此方向在一定的角度范围内变动，温度的稳定性是可以保持的.还进一步对晶体的通光长度和外加电场的方向进行了筛选，实现了双轴晶体KTP电光调制器的最优设计. 关键词： 电光效应 耦合波理论 电光调制器 最优设计     

Asymmetric Total Synthesis of (−)‐Kravanhin B

The first asymmetric total synthesis of kravanhin B has been accomplished with a linear reaction sequence of 13 steps starting from (R)‐(?)‐carvone. The synthesis features an intramolecular aldol cyclization to construct the desired cis‐fused decalin skeleton and an acid‐catalyzed dehydration and olefin isomerization to install the γ‐butenolide ring.     

C3对称性含膦三足体衍生物及其Eu(Ⅲ)配合物的合成以及与DNA相互作用的研究

设计合成了一种新的C3对称性含膦三足体衍生物N',N',N'-三(亚磷酸三乙酯)缩氨三乙酸(L)及其Eu(Ⅲ)配合物.用1H NMR、13C NMR、红外光谱、元素分析、差热-热重及紫外光谱对其组成和结构进行分析和表征.结果表明,三足体衍生物与稀土苦味酸盐(Eu(pic)3·6H2O)形成了1:1配合物Eu(pic)3L.综合运用紫外-可见吸收光谱法、荧光光谱法和循环伏安法研究了Eu(pic)3L与小牛胸腺DNA之间的结合模式,结果表明,配合物Eu(pic)3L与DNA之间以嵌插形式发生相互作用.将该配合物作为杂交探针,对其在DNA电化学传感器方面的应用进行了探讨.结果发现,该配合物在修饰单链DNA的电极检测作用下,无明显的电化学信号响应,而当将其用于检测杂交双链DNA时,出现了明显信号,并且该配合物的DNA传感器对互补序列、错配序列及非互补序列都有良好的选择作用.     

基于PCI总线的矩阵电路在压变温压补偿系统中的实现与应用

本文提出基于PCI总线驱动控制的矩阵电路在压力变送器温压补偿系统中应用的目的是解决现有压力变送器温压补偿系统中HART总线型工位电路数量少,整套矩阵电路缺失冗余性,以及现有电路在压力变送器产品温压补偿中实用性差、维护成本高的问题。文中阐述的矩阵电路是以PCI总线为基础,实现对PIO数字接口卡的驱动控制,完成由PCI总线上32路数字I/O到168路数字I/O的转换,并利用168路数字I/O进行继电器矩阵电路设计,实现了弱电控制强电的过程,成功有效的解决了现存压力变送器温压补偿系统中矩阵电路存在的问题。该研发成果已经应用于PDS压力变送器产品温压补偿生产线上,并且该电路的设计能够满足压力变送器生产企业的需求,而且整套电路融入系统中能够长期稳定、可靠的运行。     

A dual microsphere based on PLGA and chitosan for delivering the oligopeptide derived from BMP-2

In this paper, we document the process and findings of preparing dual poly (lactide-co-glycolide)/chitosan microspheres (PLGA/CS MSs) for osteoinductive oligopeptide derived from BMP-2 (abbreviated as Peptide-24). Through adjusting the amount of Peptide-24, three kinds of PLGA/CS MSs were successfully constructed in twice encapsulations. We studied the morphology, size distribution and loading efficiency of the PLGA/CS MSs. We also focused on the pH change of the environment and the molecular weight of the matrix during the degradation process of PLGA/CS MSs. More specifically, the release of Peptide-24 from three kinds of PLGA/CS MSs was monitored in PBS at 37 °C and pH 7.4. The structural stability of the released Peptide-24 was detected by Far-UV circular dichroism and MALDI-TOF-MS analysis. The mean sizes of the three kinds of PLGA/CS MSs are 47.5, 63.0 and 89.1 μm; and their drug-loading rates are 2.61, 3.21 and 2.21%, respectively. Comparing with Chitosan microspheres (abbreviated as CS MSs), the PLGA/CS MSs have excellent release curves with zero-order kinetics and controllable model. The incubation solution of PLGA/CS MSs avoided producing acid environment as poly (lactide-co-glycolide) microspheres (PLGA MSs) did, which was explained by analyzing the molecular weight of the matrix. The released oligopeptide kept its original structure and relative molecular weight throughout the procedures of encapsulation, storage and release. This indicates its structure stability. Thus, we conclude that dual PLGA/CS MSs is a promising vehicle that is suitable for the delivery of bioactive factors.     

Selected reaction monitoring (SRM) mass spectrometry without isotope labeling can be used for rapid protein quantification

The validation of putative biomarker candidates has become the major bottle-neck in protein biomarker development. Conventional immunoaffinity methods are limited by the availability of antibodies and kits. Here we demonstrate the feasibility of using selected reaction monitoring (SRM) without isotope labeling to achieve fast and reproducible quantification of serum proteins. The SRM/MRM assays for three standard serum proteins, including ceruloplasmin (CP), serum aymloid A (SAA) and sex hormone binding globulin (SHBG), have good linear ranges, generally 10(3) to 10(4) . There are almost perfect correlations between SRM intensities and the loaded peptide amounts (R(2) is usually ~0.99). Our data suggest that SRM/MRM is able to quantify proteins within the range of 0.2-2 fmol, which is comparable to the commercial ELISA/LUMINEX kits for these proteins. Excellent correlations between SRM/MRM and ELISA/LUMINEX assays were observed for SAA and SHBG (R(2)=0.928 and 0.851, respectively). However, the correlation between SRM/MRM and ELISA for CP is less desirable (R(2)=0.565). The reproducibility for SRM/MRM assays is generally very good but may depend on the proteins/peptides being analyzed (R(2)=0.931 and 0.882 for SAA and SHBG, and 0.723 for CP). The SRM/MRM assay without isotope labeling is a rapid and useful method for protein biomarker validation in a modest number of samples and is especially useful when other assays such as ELISA or LUMINEX are not available.