五磷酸镨晶体中缺陷的X形貌研究

首次报导了五磷酸镨晶体中的缺陷的Ｘ表貌研究结果，这些缺陷是铁弹畴，反相畴界，生长层和生长区界面，探讨了它们的成因及其克服办法。     

“疯牛病”与“疯人病”——蛋白粒与蛋白粒疾病

蛋白粒是一个不含核苷酸的蛋白性粒子,能够传染动物和人．引起大脑损伤及死亡．蛋白粒疾病包括羊瘙痒病、牛海绵体脑炎、人的克氏-约氏病、杰氏-斯氏-斯氏病以及致命性家族失眠症．本文从蛋白粒与人类和动物疾病的关系,回顾了蛋白粒疾病发生及传染的过程．具有不同氨基酸组成的蛋白粒,存在着可溶性的ＰｒＰC型及不溶性ＰｒＰＳＣ型．只有ＰｒＰＳＣ是传染性的．通过对蛋白粒结构与功能的剖析,讨论了蛋白粒的基因、蛋白粒的产生以及可能的致病机理（Ｘ蛋白被发现与细胞内蛋白粒增生有关）．最后,对蛋白质、ＤＮＡ和ＲＮＡ之间的遗传信息流提出了一个新的假说．     

VPA及其同系物对PrPc在小鼠胚胎干细胞表达的影响

PrP^c在小鼠胚胎干细胞诱导分化形成的胚胎小体（EBs)中有所表达，其表达水平与丙戊酸（VPA）及其衍生物（VPA-A，VPA-B，VPA-C）的DCF值、ROS产量以及VPA-E的浓度成正比，VPA及其衍生物可以使PrP^c的表达上调，抗氧化剂维生素E（V-E）和VPA共同使用，可使VPA诱发的PrP^c表达减少，VPA及其衍生物处理的（EBs)的PrP^c表达水平与它们的胚胎毒性相一致，胚胎毒性越大，PrP^c表达越多，以上结果表明，PrP^c的表达与细胞的氧化还原状态相关，PrP^c很可能参与细胞的抗氧化防御过程。     

Influence of PrP 106―126 on expression of laminin and fibronectin in astrocyte

Astrogliosis is a hallmark of prion disease, but the metabolic alterations of astrocytes remain poorly documented. A synthetic peptide corresponding to amino acid 106-126 of the human prion protein （PrP） has been shown to be toxic to neurons. In this study, the effects of PrP 106-126 on astrocytes were investigated in vitro. The proliferation of astrocytes was significantly （P 〈 0.05） increased when grown in media conditioned with PrP 106-126 （80 μmol/L） from microglia. The expression of laminin （LN） and fibronectin （FN） was examined at both mRNA and protein levels. The results showed that exposure of astrocytes to PrP 106-126 enhanced the expression of LN and FN. The increase of FN in astrocyte cultures required cytokines previously released by activated microglia. This study reveals the expression of LN and FN affected by PrP106-126.     

水貂朊蛋白前体基因的原核表达

 构建了水貂朊蛋白前体基因的表达载体,所筛选出的阳性克隆质粒经转化表达菌BL21(DE3)后,收获表达菌,纯化鉴定表明获得了目的产物.     

Cloning, sequencing and phylogenic analysis of duck prion gene

Duck prion gene was cloned and sequenced. Similar to mammalian prion protein (PrP), duck prion is encoded by a single exon of a single copy in genome, which was confirmed by Southern blot analysis. All of the structural features of mammalian PrP were also identified in the duck PrP. Compared with mammalian PrP, it exhibited a 30 % of general similarity. When compared with chicken PrP, it showed a higher homology of 97%. A phylogenetic tree was constructed to trace evolution of prion gene in animals.