岷江眉山段四川华鳊的繁殖生物学资料

于2013年3月至2014年1月对岷江眉山段四川华鳊(Sinibrama taeniatus)的繁殖生物学进行了研究。四川华鳊的繁殖时间主要集中在4~5月份,最小性成熟雌性个体体长70 mm,体重7.1 g;最小性成熟雄性体长为65 mm,体重为4.5 g。四川华鳊种群性比(雌︰雄)为1.00︰1.57,主要由4个年龄组组成,其中1龄个体数量占绝对优势。性成熟系数4~5月份最大,同期丰满度最小。卵径(1.05±0.17)mm,大小分布呈单峰型,为单批产卵型鱼类。绝对繁殖力(2 734±258)粒,相对繁殖力为(236±20)粒/g,绝对繁殖力随着鱼体长、体重增长而增大。分析显示,选择适合的渔具、渔法对保护岷江眉山段四川华鳊自然种群资源十分重要。     

野生棘胸蛙消化器官蛋白酶的分布及酶活力

本研究在不同p H和温度条件下以离体方式对野生棘胸蛙(Quasipaa spinosa)不同消化器官的蛋白酶活力进行了分析。结果表明,食道、胃、胰的蛋白酶活力受到酶体系p H的显著影响(P0.05),且随p H升高呈现典型的单峰型活力曲线。食道和胃的蛋白酶活力在p H为1.5时达到峰值,胰的酶活力在p H为9.6时达到峰值,而肠道酶活力在p H为7.4时达到峰值。各消化器官蛋白酶活力具有明显的温度依赖性(P0.05),酶活力随温度升高也均呈典型的单峰型活力曲线,不同消化器官的最大酶活力温度分别为,食道50℃、胃50℃、胰45℃、前肠45℃、后肠45℃、直肠45℃。在最大酶活力的p H和30℃条件下,各消化器官蛋白酶活力由高到低依次为胰、食道、胃、直肠、前肠、后肠。由此可见,蛋白酶在棘胸蛙消化系统的分布具有明确的规律性,且不同来源的蛋白酶需要在特定p H和温度下才能表现出最大的反应活性。     

Emerging directions in the study of the ecology and evolution of plant-animal mutualistic networks: a review

The study of mutualistic plant and animal networks is an emerging field of ecological research. We reviewed progress in this field over the past 30 years. While earlier studies mostly focused on network structure, stability, and biodiversity maintenance, recent studies have investigated the conservation implications of mutualistic networks, specifically the influence of invasive species and how networks respond to habitat loss. Current research has also focused on evolutionary questions including phylogenetic signal in networks, impact of networks on the coevolution of interacting partners, and network influences on the evolution of interacting species. We outline some directions for future research, particularly the evolution of specialization in mutualistic networks, and provide concrete recommendations for environmental managers.     

Isolation and Functional Analysis of Chalcone Isomerase Gene from Purple-Fleshed Sweet Potato

Plant Molecular Biology Reporter - Chalcone isomerase (CHI, EC 5.5.1.6) is one of the essential enzymes in the anthocyanin biosynthetic pathway catalyzing the stereospecific isomerization of...     

Conformational changes in MetNI: steered molecular dynamic studies of the methionine ABC transporter with and without substrates

ATP-binding cassette (ABC) transporters are integral membrane proteins that utilised energy from ATP hydrolysis to translocate substrates across the membrane. In addition to the common nucleotide-binding domains (NBDs) and transmembrane domains (TMDs), the methionine ABC transporter has C-terminal regulatory domains (C2 domains) that belong to ACT protein family. When the amount of methionine in the cell is high, the transport stops. This phenomenon is called trans-inhibition. To understand how a trans-inhibited protein returns to an uninhibited, resting state, we performed steered molecular dynamic simulations with and without the substrates. From the simulations, we observed some important conformational changes in the whole ABC transporter, including the constriction in the translocation pathway in the TMDs and approach of the NBDs. However, the C2 domains behaved differently in two types of the simulations. These findings might help to explain the relationship of the conformational changes of the C2 domains with the rearrangements of the NBDs or TMDs, and provide a way to understand the trans-inhibition from an opposite direction.