割草和放牧对大针茅根际与非根际土壤养分和微生物数量的影响

选取内蒙古典型草原大针茅为主要研究对象,研究割草和放牧干扰对其根际与非根际土壤有机碳、全氮、有效氮、全磷、有效磷含量以及微生物数量的影响.结果表明：在割草和放牧干扰下,根际土壤有机碳、全氮、有效氮含量均有不同程度的减少,根际截存效应减弱;土壤全磷由于固定性强不易向植物根部聚集,土壤全磷的根际效应不明显;土壤有效磷异质性较大,在放牧和割草干扰下有不同程度的变化,但根际和非根际间差异不显著;放牧干扰显著减少了土壤微生物的数量;土壤养分的变化与土壤微生物数量的变化关系密切,细菌和真菌的数量变化可能对土壤养分的影响更大;相对于割草,放牧干扰更易造成根际土壤养分的流失及微生物数量的减少.     

离子液体在天然活性物质提取中的应用研究进展

查阅近年来国内外相关文献,并进行分析、归纳和总结 , 综述离子液体在天然活性物质提取中的应用研究进展。离子液体作为一 种绿色溶剂,并以其独特性质,近年来在天然活性物质提取领域的应用研究备受关注。不过,目前用于天然活性物质提取的离子液体大 多仅为咪唑类型, 且尚未发现不同类型离子液体对不同种类天然活性成分的提取效率具有明显的特异性和规律性, 这有待进一步深入研究。     

星虫动物门活性物质及药理作用研究

本文简要介绍了星虫动物门的由来、分类和星虫的一般生理生态活性特征,并对星虫动物门的资源利用现状进行了分析,肯定了我国在星虫人工养殖、新药开发和利用其作为污染物监测方面所取得的成就.重点介绍了星虫动物门已经发现的营养活性物质、自身生理活性物质和药理活性物质以及星虫所具有的药理活性并对其未来研究进行了展望,比较了国内外学者对星虫研究的区别,为更好地保护和研究星虫提出了一些思路.     

Transformation of Gaeumannomyces graminis with β‐Glucuronidase Reporter and Hygromycin Resistance Genes

Take‐all disease is caused by Gaeumannomyces graminis, (Sacc.) Arx & D. Olivier, a soil‐borne fungus, which colonizes the root and crown tissue of many members of the Poaceae plant family. This fungus is able to grow along the surface of roots as darkly pigmented runner hyphae, which has the ability to penetrate the root. Here, we describe a genetic transformation of G. graminis var. graminis by using polyethylene glycol (PEG)‐based protoplast transformation. Fungus cells were transformed with a plasmid, pHPG, containing the gusA reporter gene that codes for β‐glucuronidase (GUS) and the hph gene for hygromycin resistance as the selectable marker. A de novo transformant selection assay was developed to identify the putative transformants that were expressing the hph gene. In addition, the transformed cells maintained the ability to infect the plant tissues. The GUS‐expressing fungus can be used to study fungal infection processes including fungal penetration, colonization and the role(s) of melanin during pathogenesis. Thus, this study is the first report of G. graminis var. graminis transformed with a visibly detectable reporter gene that provides a useful tool to a better understanding of host–Gaeumannomyces interactions.     

Conformational regulation of the EGFR kinase core by the juxtamembrane and C-terminal tail: a molecular dynamics study

The catalytic domain of epidermal growth factor receptor (EGFR) is activated by dimerization, which requires allosteric coupling between distal dimerization and catalytic sites. Although crystal structures of EGFR kinases, solved in various conformational states, have provided important insights into EGFR activation by dimerization, the atomic details of how dimerization signals are dynamically coupled to catalytic regions of the kinase core are not fully understood. In this study, we have performed unrestrained and targeted molecular dynamics simulations on the active and inactive states of EGFR, followed by principal component analysis on the simulated trajectories, to identify correlated motions in the EGFR kinase domain upon dimerization. Our analysis reveals that the conformational changes associated with the catalytic functions of the kinase core are highly correlated with motions in the juxtamembrane (JM) and C-terminal tail, two flexible structural elements that play an active role in EGFR kinase activation and dimerization. In particular, the opening and closing of the ATP binding lobe relative to the substrate binding lobe is highly correlated with motions in the JM and C-terminal tail, suggesting that ATP and substrate binding can be coordinated with dimerization through conformational changes in the JM and C-terminal tail. Our study pinpoints key residues involved in this conformational coupling, and provides new insights into the role of the JM and C-terminal tail segments in EGFR kinase functions.     

Structural analysis of CPF_2247, a novel α-amylase from Clostridium perfringens

CPF_2247 from Clostridium perfringens ATCC 13124 was identified as a putative carbohydrate‐active enzyme by its low sequence identity to endo‐β‐1,4‐glucanases belonging to family 8 of the glycoside hydrolase classification. The X‐ray crystal structure of CPF_2247 determined to 2.0 Å resolution by single‐wavelength anomalous dispersion using seleno‐methionine‐substituted protein revealed an (α/α)₆ barrel fold. A large cleft on the surface of the protein contains residues that are structurally conserved with key elements of the catalytic machinery in clan GH‐M glycoside hydrolases. Assessment of CPF_2247 as a carbohydrate‐active enzyme disclosed α‐glucanase activity on amylose, glycogen, and malto‐oligosaccharides. Proteins 2011;. © 2011 Wiley‐Liss, Inc.     

Crystal structure and substrate-binding mode of cellulase 12A from Thermotoga maritima

Cellulases have been used in many applications to treat various carbohydrate-containing materials. Thermotoga maritima cellulase 12A (TmCel12A) belongs to the GH12 family of glycoside hydrolases. It is a β-1,4-endoglucanase that degrades cellulose molecules into smaller fragments, facilitating further utilization of the carbohydrate. Because of its hyperthermophilic nature, the enzyme is especially suitable for industrial applications. Here the crystal structure of TmCel12A was determined by using an active-site mutant E134C and its mercury-containing derivatives. It adopts a β-jellyroll protein fold typical of the GH12-family enzymes, with two curved β-sheets A and B and a central active-site cleft. Structural comparison with other GH12 enzymes shows significant differences, as found in two longer and highly twisted β-strands B8 and B9 and several loops. A unique Loop A3-B3 that contains Arg60 and Tyr61 stabilizes the substrate by hydrogen bonding and stacking, as observed in the complex crystals with cellotetraose and cellobiose. The high-resolution structures allow clear elucidation of the network of interactions between the enzyme and its substrate. The sugar residues bound to the enzyme appear to be more ordered in the -2 and -1 subsites than in the +1, +2 and -3 subsites. In the E134C crystals the bound -1 sugar at the cleavage site consistently show the α-anomeric configuration, implicating an intermediate-like structure.