用Monte Carlo方法设计X射线均整器

在以电子直线加速器为X射线源的工业CT和辐射治疗中,需要较均匀的X射线剂量率空间分布。利用MonteCarlo方法,设计了6MeV和9MeV的X射线均整器。对9MeV的X射线均整器进行了实验。实验结果表明:在距靶1m处测得均整后0°处的剂量率约为均整前的74%,7.5°处的剂量率约为0°处的69%。满足Varian标准。该均整器在满足平坦度要求的同时提高X射线剂量利用率,不经过打磨便可得到较好的均整结果。     

Tm值差异型不对称PCR方法的建立及其在分子诊断中的应用

多数分子诊断方法对靶基因的检测都是以单链DNA为基础的,如何获得大量和高质量的单链靶DNA分子一直是研究热点.以包含BRCA1基因上3个单核苷酸多态性(SNP)的DNA片段为研究对象,通过调整不对称扩增引物碱基序列组成(5′-端引入错配或加入锁核苷酸(locked nucleic acid,LNA)),使用相差10倍浓度来增加不对称引物间Tm值差异,改进扩增条件(添加增强剂的扩增缓冲液,不同退火温度的二阶循环扩增程序)后,进行不对称扩增来产生大量单链靶DNA产物.结果表明Tm差异型不对称PCR(Tm difference asymmetric PCR,TDA-PCR)可有效提高单链DNA分子产率,降低引物设计难度,也扩大了模板序列的适用范围.此外,还针对禽流感病毒H5N1的血凝素(haemagglutinin)HA基因保守序列进行不对称扩增,用获得的单链DNA为模板进行焦磷酸测序检测,所得结果与参考序列一致且无明显干扰信号.因此,采用Tm值差异型不对称PCR可使焦磷酸测序等分子诊断流程更为简便,成本更低,效率更高,具有很好的通用性和实用性.     

鳄蜥皮肤光镜与扫描电镜观察

光镜观察，鳄蜥皮肤由深层到表面，依次是生发层、中间层、α角质层、β角质层和角皮层。扫描电镜３５００倍观察，皮肤鳞片角皮层具有小刺和小窝的细微结构，小刺长８２．４μｍ，基部直径为９．１２μｍ；２０００倍观察另一小刺长１４．６μｍ，基部直径为２．７μｍ，小窝直径为１６μｍ，小刺和窝在角皮层上是零星分布。     

有限温度时的二维界面极化子

用类Ｌｅｅ－Ｌｏｗ－Ｐｉｎｅｓ中间耦合方法讨论了在有限温度情形极性－极性半导体异质结中界面极化子的性质．在二维近似下，得到了两支界面光学声子模影响下的极化子能量和有效质量的解析表达式．结果表明：极化子效应随温度的升高而减弱，并发现极化子能量较其有效质量对温度更为敏感．数值结果表明温度效应对某些Ⅱ－Ⅵ族半导体异质结是重要的，但对Ⅲ－Ⅴ族半导体异质结是不重要的．     

环烷酸—TBP系分离提纯La_2O_3的研究

采用环烷酸—TBP体系对混合稀土中的La进行分离提纯。测定了La、Ce、Y、Pr、Gd、Nd的pH_(1/2)值,以及,并据此设计出分馏萃取流程。经试验,确定用20级萃取和10级洗涤,所得La_2O_3产品的纯度可达99.95％,收率为97％。环烷酸—TBP体系具有无臭、分层快、粘度小、成本低等优点,可用来代替常用的P_(350)、P_(507),作为分离提纯La的萃取剂。     

Genistein inhibits human TNF-α-induced porcine endothelial cell adhesiveness for human monocytes and natural killer cells

Cellular immune response is a major barrier to xenotransplantation. Human tumor necrosis factor-α (hTNF-α) possesses cross-species activity and directly amplifies the immune rejection via the upregulation of adhesion molecules on porcine endothelium. We investigated the role of protein tyrosine phosphorylation in the induction of expression of E-sclectin and vascular cell adhesion molecule-1 (VCAM-1), and the augmentation of adhesion of human peripheral blood monocytes (PBMo) and natural killer cells (PBNK), after rhTNF-α-stimulation of porcine aortic endothelial cells (PAEC) in vitro, rhTNF-α-increased adhesiveness of PAEC for both PBMo and PBNK was dose-dependently reduced by pretreatment of PAEC with the selective protein tyrosine kinase (PTK) inhibitor genistein. The inhibitory effect occurred at the early time of PAEC activation triggered by rhTNF-α, and was completely reversible. PTK activity assay indicated that genistein also suppressed rhTNF-α stimulated activation of protein tyrosine kinases (PTKs) in PAEC in a dose-dependent manner. Flow cytometric analysis showed that genistein inhibited the upregulation of E-selectin and VCAM-1 by rhTNF-α. These results suggest that PTKs may regulate the expression of E-selectin and VCAM-1 on PAEC and the adherence of PBMo and PBNK induced by rhTNF-α. Moreover, dietary genistein, used as an adhesion antagonist, may contribute to managing the cell-mediated rejection in the clinical application.     

具有循环中心和小中心商的有限p群

本文证明中心循环且中心商为p~5阶群的有限p群能分为15个互不同构的类。     

Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state. Here we present a 2.7 A crystal structure of Escherichia coli trigger factor, the best-characterized chaperone of this type, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit. Trigger factor adopts a unique conformation resembling a crouching dragon with separated domains forming the amino-terminal ribosome-binding 'tail', the peptidyl-prolyl isomerase 'head', the carboxy-terminal 'arms' and connecting regions building up the 'back'. From its attachment point on the ribosome, trigger factor projects the extended domains over the exit of the ribosomal tunnel, creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation. This study sheds new light on our understanding of co-translational protein folding, and suggests an unexpected mechanism of action for ribosome-associated chaperones.