蛋白质微阵列技术及其影响因素的研究进展

简要介绍了蛋白质微阵列技术的基本原理和制备技术。重点讨论了蛋白质微阵列在制备和检测过程中的主要影响因素,如载体及其表面处理、探针、检测方法、制备技术等。指出蛋白质微阵列是一种极具发展前途的新型研究工具,在我国刚刚起步,需要加大投入和合理规划。     

飞行仿真器综合显示系统关键技术研究

介绍了综合显示系统的概念,以及国内外发展的现状;提出了在飞行仿真器平台上综合显示系统的框架结构,并研究了其中的关键技术。采用模糊逻辑推理算法实现多传感器/多数据源、多分辨率信息的数据融合;图像融合方面主要处理了二维显示与三维显示并存的问题;在系统的设计和实现上,运用了组件化的思想和技术。最后,概述了综合显示系统的发展趋势。     

Protein aggregation as primary and characteristic cell reaction to various stresses

Ehrlich carcinoma and EL-4 thymoma ascites cells were subjected in vitro to heat shock, ATP depletion, oxidative stress, Ca²⁺ overlading and iodoacetamide treatment. After the transient stresses, Triton (X-100)-insoluble TIS) fractions were isolated from the cells and analysed by electrophoresis and immunoblotting. All stresses used caused rapid aggregation of cell proteins. This was manifested in a signficant rise in protein content in the TIS fractions. The protein increase was mostly due to and increase in the insolubility of actin, 57 kDa protein of intermediate filaments, 70 kDa heat shock protein (HSP 70), and some specific proteins whose insolubilization was a characteristic sign for each type of cell injury. Different survival rates in the cell lines after either stress corrlated well with differences in their TIS protein accretion. Possible mechanisms for stress-induced protein aggregation and its relationship with cell viability are suggested.     

新疆五种芫菁血淋巴蛋白质谱带的比较研究

本文报道了用聚丙烯酰胺凝胶电泳法分析比较了新疆常见五种芫菁血淋巴蛋白质的谱带.研究结果表明,血淋巴蛋白质谱带具有明显种属特异性,属间差异明显大于种间差异.     

猪血蛋白源利用初探

1.采用动物酶一次性水解猪全血与干血粉获得含17种氨基酸的水解物,蛋白质含量达83.33%。对该水解物进行了氨氮、总氮、蛋白质含量、氨基酸组成的一系列分析。以水解物连续饲养小白鼠30天,未见毒性,分析饲喂30天后的小白鼠血浆蛋白及 SH 含量,发现血清蛋白含量增长,SH 含量未见变化.30天后肝组织重量及指数不变,解剖观察小白鼠也未见病变.进一步说明水解物无毒性,唯免疫器官脾脏增大21%,最后以1%浓度水解物添加普通酱油,结果提高氨氮32.43%.2.对比研究了硫酸水解猪血粉提制复合氨基酸工艺,又研究了猪血蛋白质水解液用石灰乳脱酸制备复合 L—氨基酸的方法。     

Role of <Emphasis Type="Italic">N</Emphasis>-linked polymannose oligosaccharides in targeting glycoproteins for endoplasmic reticulum-associated degradation

Misfolded or incompletely assembled multisubunit glycoproteins undergo endoplasmic reticulum-associated degradation (ERAD) regulated in large measure by their N-linked polymannose oligosaccharides. In this quality control system lectin interaction with Glc₃Man₉GlcNAc₂ glycans after trimming with endoplasmic reticulum (ER) -glucosidases and -mannosidases sorts out persistently unfolded glycoproteins for N-deglycosylation and proteolytic degradation. Monoglucosylated (Glc₁Man₉GlcNAc₂) glycoproteins take part in the calnexin/calreticulin glucosylation-deglucosylation cycle, while the Man₈GlcNAc₂ isomer B product of ER mannosidase I interacts with EDEM. Proteasomal degradation requires retrotranslocation into the cytosol through a Sec61 channel and deglycosylation by peptide: N-glycosidase (PNGase); in alternate models both PNGase and proteasomes may be either free in the cytosol or ER membrane-imbedded/attached. Numerous proteins appear to undergo nonproteasomal degradation in which deglycosylation and proteolysis take place in the ER lumen. The released free oligosaccharides (OS) are transported to the cytosol as OS-GlcNAc₂ along with similar components produced by the hydrolytic action of the oligosaccharyltransferase, where they together with OS from the proteasomal pathway are trimmed to Man₅GlcNAc₁ by the action of cytosolic endo--N-acetylglucosaminidase and -mannosidase before entering the lysosomes. Some misfolded glycoproteins can recycle between the ER, intermediate and Golgi compartments, where they are further processed before ERAD. Moreover, properly folded glycoproteins with mannose-trimmed glycans can be deglucosylated in the Golgi by endomannosidase, thereby releasing calreticulin and permitting formation of complex OS. A number of regulatory controls have been described, including the glucosidase-glucosyltransferase shuttle, which controls the level of Glc₃Man₉GlcNAc₂-P-P-Dol, and the unfolded protein response, which enhances synthesis of components of the quality control system.Received 26 January 2004; accepted 25 February 2004     

Protein folding revisited. A polypeptide chain at the folding – misfolding – nonfolding cross-roads: which way to go?

The structure-function paradigm claims that a specific function of a protein is determined by its unique and rigid three-dimensional (3D) structure. Thus, following its biosynthesis on the ribosome, a protein must fold to be functional. This idea represents one of the cornerstones of modern biology. Numerous cases when, due to the effect of environmental factors or because of genetic defects (mutations), a polypeptide chain has lost its capability to gain a proper functional 3D structure (i.e. became misfolded), seem to confirm this concept. Consequences of such misfolding are well known and represent lost of function, aggregation, development of conformational disorders and cell death. However, the recent revelation of countless examples of intrinsically disordered proteins has cast doubt on the general validity of the structure-function paradigm and revealed an intriguing route of functional disorder. Thus, in a living cell, a polypeptide chain chooses between three potential fates – functional folding, potentially deadly misfolding and mysterious nonfolding. This choice is dictated by the peculiarities of amino acid sequence and/or by the pressure of environmental factors. The aim of the present review is to outline some interesting features of these three routes.Received 5 March 2003; received after revision 28 March 2003; accepted 31 March 2003     

Protein folding: concepts and perspectives

In this review, the main concepts of protein folding, as deduced from both theoretical and experimental in vitro studies, are presented. The thermodynamic aspects from Anfinsen's postulate, Levinthal's paradox to the concept of folding funnel as proposed by Wolynes and coworkers are described. Concerning the folding pathway(s), particular attention is brought to bear on the early steps that initiate the process in the light of the results of the fast and even ultrafast techniques presently being used. The role of structural domains as folding units is discussed. Last, from the recent studies, it can be concluded that the main rules deduced from the in vitro folding studies are valid for the folding of a nascent polypeptide chain in vivo.     

二阶导数光谱法测定蛋白质的含量

导数光谱是紫外可见分光光度法中用以排除干扰的一种技术。本文用日立220—A紫外可见分光光度计中测定了血清蛋白质的含量。通过实验得出的线性回归方程为D=155.24c—0.346;相关系数r=0.9998,样本平均回收率为100.05％,精度试验d=0.077,S=0.418,dx=0.027,Sx=0.148。此法重现好,变异系数(CV)<±1％,此法简单,快速,可用于血清蛋白质的测定。     

面向Yarn规范的蛋白质折叠模拟计算并行化算法

为了提高生物信息学中蛋白质折叠模拟计算的速度,提出了面向Yarn(Yet Another Resource Negotiator)规范的蛋白质折叠模拟计算并行化算法Yarn_PERM。分析了蛋白质折叠的格点模型PERM算法的运行流程及其面向Map-Reduce的子任务划分方式。Yarn_PERM算法实现采用Hadoop2.0的Yarn框架作为工作平台,其资源的分配与调度、应用子任务的申请和子任务的具体执行都由Yarn来透明的完成;描述了Yarn_PERM算法的Map程序与Reduce程序及主控程序的功能实现。选择了一个有代表性的蛋白质序列数据作为案例程序进行了测试。实验结果表明：在相同的时间内Yarn_PERM比PERM串行计算、Map-Reduce的PERMS计算在能量最低寻优的吞吐量上明显增加,加速比和可扩展性上也有明显的优势。