黄瓜香水、醇提取液对肠道菌群的调整作用的比较

目的研究不同溶剂提取黄瓜香有效成分的作用效果,以期能更好提高药物的利用度。方法用盐酸林可霉素制造小鼠菌群失调模型,然后分别用黄瓜香的水、醇提取物治疗,比较治疗效果。结果醇提取物和水提取物均能调整肠道菌群平衡,与自然恢复组相比差异有统计学意义(P0.05),且醇提取物组效果要优于水提取物组(P0.05)。结论黄瓜香醇提取物是理想的微生态调节剂。     

牛肾组织及其培养物的不同消化法效果评价

为了比较不同消化液及消化方式对牛肾皮质组织和培养后形成单层细胞的消化分散效果并确定最适消化液和消化方式,分别用0.25%胰蛋白酶和0.25%胰蛋白酶-0.02%EDTA两种消化液,消化牛肾皮质组织及其培养形成的单层牛肾皮质细胞。牛肾皮质组织采用热(37℃)和冷(4℃)两种消化方式;经培养形成单层的牛肾皮质细胞采用室温(25℃)消化。结果显示,用0.25%胰蛋白酶-0.02%EDTA消化液热消化牛肾组织时,分散获得牛肾皮质细胞的活细胞数、存活率、贴壁率均优于其他消化方法,差异显著(P0.05)。培养形成的单层牛肾皮质细胞用0.25%胰蛋白酶-0.02%EDTA消化液的消化速度明显快于用单一0.25%胰蛋白酶消化液的消化速度,统计学分析显示具有显著性差异(P0.01),两种消化液消化所得细胞的存活率及贴壁率前者要更高,差异显著(P0.05)。     

盐胁迫下镧对水稻幼苗生长的保护效应

通过液培实验,研究水稻幼苗在盐胁迫下,镧对水稻幼苗的保护作用。结果表明：水稻幼苗植株在≤1．5％的盐浓度的盐胁迫下,10mg·L^-1镧能提高幼苗植株超氧化物歧化酶（SOD）和过氧化氢酶（CAT）的活性;降低幼苗植株脂质过氧化产物丙二醛（MDA）的含量和脯氨酸（Pro）的含量;减小质膜透性;提高叶片叶绿素含量和叶绿素a／b的比值;增强根系的活力,进而促进水稻幼苗的生长。10mg·L^-1镧对盐胁迫的缓解作用与盐浓度有关,随着盐浓度增大,镧的缓解作用将逐渐消失。分析表明,在≤1．0％和≥0．5％的盐浓度胁迫下,镧对水稻幼苗的生长存在更有效的防御机制,能够促进水稻幼苗的生长代谢。     

淮河淮南段与巢湖水质污染对鲫鱼（Carassius auratus）的毒性效应

研究了枯水期淮河淮南段及巢湖西半湖水质污染对鲫鱼的毒性效应。从淮河淮南段与巢湖采集鱼类样本,并以未受人为污染的安丰塘鱼类为对照,分析了鲫鱼肝脏丙二醛（Malondialdehyde,MDA）含量、超氧化物歧化酶（Superoxide dismutase,SOD）活性、谷胱甘肽硫转移酶（Glutathione S-transferase,GST）活性、7-乙氧基异吩恶唑-O-脱乙基酶（7-ethoxyresorufin-O-deethylase,EROD）活性及DNA单链损伤情况,结果表明,淮河淮南段鲫鱼肝脏MDA含量、SOD活性、GST活性、EROD活性均高于对照组,分别是对照组的2.88、1.48、2.03和3.93倍;巢湖鲫鱼肝脏MDA含量、SOD活性、EROD活性均高于对照组,分别是对照组的2.28、1.85和2.74倍。肝细胞DNA单链断裂的测定显示淮河淮南段与巢湖的水质污染均对鲫鱼有遗传毒性。     

Heritability of resistance to oxidative stress in early life

Oxidative stress has recently been suggested to play an important role in life‐history evolution, but little is known about natural variation and heritability of this physiological trait. Here, we explore phenotypic variation in resistance to oxidative stress of cross‐fostered yellow‐legged gull (Larus cachinnans) chicks. Resistance to oxidative stress was not related to plasma antioxidants at hatching, which are mostly derived from maternal investment into eggs. Common environmental effects on phenotypic variation in resistance to oxidative stress were not significant. Heritability was relatively low and nonsignificant in hatchlings, but interestingly, the chicks of age 8 days showed high and significant heritability (h² = 0.59). Our results suggest that resistance to oxidative stress is determined mainly by the genotype as chicks grow. Further work is required to explore the genetic role of oxidative stress in life‐history evolution.     

Cascading extinctions, functional complementarity, and selection in two-trophic-level model communities: A trait-based mechanistic approach

The influence of diversity on ecosystem functioning and ecosystem services is now well established. Yet predictive mechanistic models that link species traits and community-level processes remain scarce, particularly for multitrophic systems. Here we revisit MacArthur's classical consumer resource model and develop a trait-based approach to predict the effects of consumer diversity on cascading extinctions and aggregated ecosystem processes in a two-trophic-level system. We show that functionally redundant efficient consumers generate top-down cascading extinctions. This counterintuitive result reveals the limits of the functional redundancy concept to predict the consequences of species deletion. Our model also predicts that the biodiversity-ecosystem functioning relationship is different for different ecosystem processes and depends on the range of variation of consumer traits in the regional species pool, which determines the sign of selection effects. Lastly, competition among resources and consumer generalism both weaken complementarity effects, which suggests that selection effects may prevail at higher trophic levels. Our work emphasizes the potential of trait-based approaches for transforming biodiversity and ecosystem functioning research into a more predictive science.     

Human RegIV Protein Adopts a Typical C-Type Lectin Fold but Binds Mannan with Two Calcium-Independent Sites

Human RegIV protein, which contains a sequence motif homologous to calcium-dependent (C-type) lectin-like domain, is highly expressed in mucosa cells of the gastrointestinal tract during pathogen infection and carcinogenesis and may be applied in both diagnosis and treatment of gastric and colon cancers. Here, we provide evidence that, unlike other C-type lectins, human RegIV binds to polysaccharides, mannan, and heparin in the absence of calcium. To elucidate the structural basis for carbohydrate recognition by NMR, we generated the mutant with Pro91 replaced by Ser (hRegIV-P91S) and showed that the structural property and carbohydrate binding ability of hRegIV-P91S are almost identical with those of wild-type protein. The solution structure of hRegIV-P91S was determined, showing that it adopts a typical fold of C-type lectin. Based on the chemical shift perturbations of amide resonances, two calcium-independent mannan-binding sites were proposed. One site is similar to the calcium-independent sugar-binding site on human RegIII and Langerin. Interestingly, the other site is adjacent to the conserved calcium-dependent site at position Ca-2 of typical C-type lectins. Moreover, model-free analysis of ¹⁵N relaxation parameters and simplified Carr-Purcell-Meiboom-Gill relaxation dispersion experiments showed that a slow microsecond-to-millisecond time-scale backbone motion is involved in mannan binding by this site, suggesting a potential role for specific carbohydrate recognition. Our findings shed light on the sugar-binding mode of Reg family proteins, and we postulate that Reg family proteins evolved to bind sugar without calcium to keep the carbohydrate recognition activity under low-pH environments in the gastrointestinal tract.     

Structure of Avian Thymic Hormone, a High-Affinity Avian β-Parvalbumin, in the Ca-Free and Ca-Bound States

Originally isolated on the basis of its capacity to stimulate T-cell maturation and proliferation, avian thymic hormone (ATH) is nevertheless a parvalbumin, one of two β-lineage isoforms expressed in birds. We recently learned that addition of Ca²⁺-free ATH to a solution of 8-anilinonaphthalene-1-sulfonate (ANS) markedly increases ANS emission. This behavior, not observed in the presence of Ca²⁺, suggests that apolar surface area buried in the Ca²⁺-bound state becomes solvent accessible upon Ca²⁺ removal. In order to elucidate the conformational alterations that accompany Ca²⁺ binding, we have obtained the solution structure of the Ca²⁺-free protein using NMR spectroscopy and compared it to the Ca²⁺-loaded protein, solved by X-ray crystallography. Although the metal-ion-binding (CD-EF) domains are largely coincident in the superimposed structures, a major difference is observed in the AB domains. The tight association of helix B with the E and F helices in the Ca²⁺-bound state is lost upon removal of Ca²⁺, producing a deep hydrophobic cavity. The B helix also undergoes substantial rotation, exposing the side chains of F24, Y26, F29, and F30 to solvent. Presumably, the increase in ANS emission observed in the presence of unliganded ATH reflects the interaction of these hydrophobic residues with the fluorescent probe. The increased solvent exposure of apolar surface area in the Ca²⁺-free protein is consistent with previously collected scanning calorimetry data, which indicated an unusually low change in heat capacity upon thermal denaturation. The Ca²⁺-free structure also provides added insight into the magnitude of ligation-linked conformational alteration compatible with a high-affinity metal-ion-binding signature. The exposure of substantial apolar surface area suggests the intriguing possibility that ATH could function as a reverse Ca²⁺ sensor.     

Structural Basis of the Regulation of the CbpA Co-chaperone by its Specific Modulator CbpM

CbpA, one of the Escherichia coli DnaJ homologues, acts as a co-chaperone in the DnaK chaperone system. Despite its extensive similarity in domain structure and function to DnaJ, CbpA has a unique and specific regulatory mechanism mediated through the small protein CbpM. Both CbpA and CbpM are highly conserved in bacteria. Earlier studies showed that CbpM interacts with the N-terminal J-domain of CbpA inhibiting its co-chaperone activity but the structural basis of this interaction is not known. Here, we have combined NMR spectroscopy, site-directed mutagenesis and surface plasmon resonance to characterize the CbpA/CbpM interaction at the molecular level. We have determined the solution structure of the CbpA J-domain and mapped the residues that are perturbed upon CbpM binding. The NMR data defined a broad region on helices α2 and α3 as involved in the interactions. Site-directed mutagenesis has been used to further delineate the CbpA J-domain/CbpM interface. We show that the binding sites of CbpM and DnaK on CbpA J-domain overlap, which suggests a competition between DnaK and CbpM for binding to CbpA as a mechanism for CbpA regulation. This study also provides the explanation for the specificity of CbpM for CbpA versus DnaJ, by identifying the key residues for differential binding.     

Solution NMR Studies of Chlorella Virus DNA Ligase-adenylate

DNA ligases are essential guardians of genome integrity by virtue of their ability to recognize and seal 3′-OH/5′-phosphate nicks in duplex DNA. The substrate binding and three chemical steps of the ligation pathway are coupled to global and local changes in ligase structure, involving both massive protein domain movements and subtle remodeling of atomic contacts in the active site. Here we applied solution NMR spectroscopy to study the conformational dynamics of the Chlorella virus DNA ligase (ChVLig), a minimized eukaryal ATP-dependent ligase consisting of nucleotidyltransferase, OB, and latch domains. Our analysis of backbone ¹⁵N spin relaxation and ¹⁵N,¹H residual dipolar couplings of the covalent ChVLig-AMP intermediate revealed conformational sampling on fast (picosecond to nanosecond) and slow timescales (microsecond to millisecond), indicative of interdomain and intradomain flexibility. We identified local and global changes in ChVLig-AMP structure and dynamics induced by phosphate. In particular, the chemical shift perturbations elicited by phosphate were clustered in the peptide motifs that comprise the active site. We hypothesize that phosphate anion mimics some of the conformational transitions that occur when ligase-adenylate interacts with the nick 5′-phosphate.