天然和人工固沙灌木林蜘蛛和甲虫分布与环境因子的关系

干旱区人工植被恢复驱动的土地利用变化强烈影响了地表和土栖的节肢动物群落结构及多样性。然而,我们对地表节肢动物群落关键类群-蜘蛛和甲虫对固沙植被恢复的响应及与环境变化关系的认识还很有限。以天然固沙灌木林和2种人工固沙灌木林为研究对象,运用方差分析和多变量分析等方法定量研究了干旱区天然和人工固沙植被区地表蜘蛛和甲虫分布特征及影响要素。结果表明,天然灌木林与人工梭梭、柽柳林地表蜘蛛和甲虫群落组成明显不同,人工梭梭、柽柳林地表蜘蛛活动密度和甲虫多样性均显著高于天然灌木林,而地表甲虫密度和蜘蛛多样性变化与之相反。两种人工固沙灌木林之间蜘蛛和甲虫群落组成也存在一定差异,人工柽柳林地表蜘蛛活动密度、多样性和甲虫物种丰富度均显著高于人工梭梭林。进一步分析发现,蜘蛛群落中狼蛛科、平腹蛛科、皿蛛亚科和球蛛科与甲虫群落中拟步甲科、步甲科和象甲科等一些甲虫种属对3种生境的选择模式不同决定了蜘蛛和甲虫群落聚集结构。植被、土壤环境因子与蜘蛛和甲虫pRDA和pCCA结果表明,草本生物量、凋落物量、土壤含砂量、电导率和灌木盖度是影响蜘蛛分布的主要环境因子,它们解释了82.1%的蜘蛛群落变异;灌木盖度、草本生物量、土壤...     

不同温度、气体微环境对红托竹荪干品储藏品质的影响

本研究针对红托竹荪干品在储藏过程中易发生褐变、降低商品性问题,探究了不同储藏条件(温度、气体微环境)对红托竹荪干品储藏品质的影响。以红托竹荪干品为原材料,考察了在气体微环境(空气、N₂、CO₂和脱氧)和不同储藏温度(5、25和45 ℃)下红托竹荪干品储藏品质的动态变化。在60 d的储藏期内,所有样品的褐变指数、剪切力、多酚氧化酶、过氧化氢酶、总酚、还原糖和5-羟甲基糠醛含量均增加,游离氨基酸、白度值、复水比均降低。与25、45 ℃相比,以上指标在5 ℃条件下均表现最优,5 ℃储藏条件下呈味氨基酸和挥发性成分指标更接近于0 d;在不同气体微环境比较下,CO₂储藏环境下干品品质保持最好,通过综合评分得出5 ℃低温结合CO₂充气条件下干品品质最优,其次为N₂结合5 ℃低温。结合经济成本,5 ℃低温结合CO₂或N₂充气可以作为红托竹荪干品延长货架期的推荐储藏技术。     

3种香薷属植物染色体数目与核型分析

参照植物根尖细胞学研究的方法标准,对香薷属3种(5个居群)植物进行核形态学分析。结果表明:(1)从染色体数目看,密花香薷2居群染色体数目2n=16;野苏子2居群染色体数目2n=20,染色体数目和倍性与前人报道的一致;毛穗香薷染色体数目2n=10为首次报道。(2)聚类分析结果显示,3种(5居群)植物中野苏子和密花香薷亲缘关系较近;结合现有报道数据分析表明,该属植物仅有2种倍性(二倍体和四倍体),且二倍体占主导地位。(3)核型参数分析表明:密花香薷的稻城无名山居群1核型公式为2n=2x=16=14m+2sm,居群2为2n=2x=16=16m,着丝粒指数(CI)分别为39.57和42.32,不对称系数AI值分别为2.75和2.87,核型不对称性都为1A型;毛穗香薷的核型公式为2n=2x=10=10m,着丝粒指数(CI)为41.76,不对称系数AI值为5.25,核型不对称性为1B型;野苏子的昆明西山居群核型公式为2n=2x=20=14m+6sm,聂拉木樟木沟居群为2n=2x=20=16m+4sm,着丝粒指数(CI)分别为38.49和40.97,不对称系数AI值为4.20和4.30,核型不对称性为1B型和2B型。     

坡向与龄级对新疆野核桃自然保护区野核桃病害的影响

为了解渐危植物新疆野核桃的病害情况,在新疆野核桃自然保护区调查不同坡向、不同龄级野核桃4种病害的患病比例,分析病害种类、病害等级与野核桃胸径及坡向的相关关系。结果表明: 保护区野核桃的主要病害为核桃褐斑病(95.8%)、核桃枯枝病(90.5%)、核桃黑斑病(74.4%)和核桃腐朽病(7.7%)。4个坡向的野核桃均易患核桃褐斑病,阴坡和半阴坡的野核桃易患核桃枯枝病,阳坡和阴坡的野核桃易患核桃黑斑病,半阳坡和半阴坡的野核桃相对易患核桃腐朽病。4个坡向野核桃的4种病害均随病害等级(1～4级)的增加而病株比例减小。4个坡向核桃枯枝病、核桃黑斑病、核桃褐斑病均以中龄树比例最大,其次是老龄树,再次是小树,未见幼苗患病;核桃腐朽病仅发生在老龄树。核桃枯枝病、核桃腐朽病、核桃黑斑病、核桃褐斑病与野核桃的胸径呈显著正相关,核桃黑斑病与坡向呈显著负相关,核桃枯枝病、核桃腐朽病、核桃黑斑病的不同病害等级与胸径和坡向存在相关性。     

Stress protein of cyanobacteria CP36: interaction with photoactive complexes and formation of supramolecular structures

Cyanobacterium Anacystis nidulans R2, Synechocystis sp. PCC 6803 (wild-type strain and mutants Delta2 and Delta3 lacking PSII and PSI, respectively), and Synechocystis sp. BO 9201 synthesize the pigment--protein complex CP36 (CPIV-4, CP43') under iron deficiency in the medium. Accumulation of CP36 is accompanied by structural reorganizations in the photosynthetic membranes. Integrating mean times of excitation relaxation (quenching) are 2.2 nsec (CP36), 1 nsec (PSI), and 420 psec (PSII in Fm state). The energy migration between CP36 and the photosystems can be described by a model of a one-layer ring of CP36 around core-complexes. The excitation from CP36 to PSI is transferred within <10 psec. The energy transfer from CP36 to PSII occurs during 170 psec. Cells with low content of CP36 probably contain only a latent fraction of unbound to phycobilisomes PSII which is the analog of PSIIbeta of higher plants. In PSI there are four binding sites for CP36 monomers per RC. PSII can bind up to 32 molecules of CP36 per RC. Cells with a large amount of CP36 contain monomer form of PSII core-complex which can bind eight tetramers of CP36 (8 binding sites). In conditions of iron deficiency only one monomer of a dimer PSII core-complex is destroyed and released chlorophyll is accumulated in CP36. Accumulation of CP36 in A. nidulans cells can be accompanied by membrane stacking which is similar to the stacking in chlorophyll b-containing organisms. The stacking can occur in the region of localization of PSII latent fraction bound to CP36. The membrane stacking shields PSII stromal surfaces from the aqueous phase for activation of electron transfer on the acceptor side of PSII.     

Food web structure in the high Arctic Canada Basin: evidence from δ13C and δ15N analysis

The food-web structure of the Arctic deep Canada Basin was investigated in summer 2002 using carbon and nitrogen stable isotope tracers. Overall food-web length of the range of organisms sampled occupied four trophic levels, based on 3.8 trophic level enrichment (¹⁵N range: 5.3–17.7). It was, thus, 0.5–1 trophic levels longer than food webs in both Arctic shelf and temperate deep-sea systems. The food sources, pelagic particulate organic matter (POM) (¹³C=–25.8, ¹⁵N=5.3) and ice POM (¹³C=–26.9, ¹⁵N=4.1), were not significantly different. Organisms of all habitats, ice-associated, pelagic and benthic, covered a large range of ¹⁵N values. In general, ice-associated crustaceans (¹⁵N range 4.6–12.4, mean 6.9) and pelagic species (¹⁵N range 5.9–16.5, mean 11.5) were depleted relative to benthic invertebrates (¹⁵N range 4.6–17.7, mean 13.2). The predominantly herbivorous and predatory sympagic and pelagic species constitute a shorter food chain that is based on fresh material produced in the water column. Many benthic invertebrates were deposit feeders, relying on largely refractory material. However, sufficient fresh phytodetritus appeared to arrive at the seafloor to support some benthic suspension and surface deposit feeders on a low trophic level (e.g., crinoids, cumaceans). The enriched signatures of benthic deposit feeders and predators may be a consequence of low primary production in the high Arctic and the subsequent high degree of reworking of organic material.     

Human T cells recognize polymorphic and non-polymorphic regions of the Plasmodium falciparum circumsporozoite protein.

In order to characterize T cell epitopes in the Plasmodium falciparum circumsporozoite (CS) protein sequence, we isolated T cell clones, from non-immune donors, which reacted with synthetic peptides corresponding to two predicted CS protein T cell epitopes. Peptide CS.T3 (corresponding to a non-polymorphic region of the CS protein, residues 378-398) was recognized in association with either DR2 or DRw9 restriction elements. T cell clones recognizing CS.T3 also reacted with the sporozoite-derived CS protein. Peptide CS.T2 corresponds to a polymorphic region (residues 325-341) of the CS protein. Unlike the CS.T3-specific clones, the CS.T2-specific clones did not recognize the CS protein. Since the CS.T2 peptide includes residues which are polymorphic in different P. falciparum isolates, we investigated whether these residues were critical for recognition of the peptide. We show here that a single amino acid substitution at a position of the CS protein which shows genetic polymorphism affects recognition of the sequence by human T cells. The implications of these data for malaria vaccine development are discussed.