福建省栗树害虫的考查(Ⅱ)

本文记载福建省栗树害虫计昆虫纲 3目 ,6 6科 ,及蛛形纲蜱螨亚纲 1目 2科。考查 ( )( )两篇合计福建省栗树害虫约 2 90种。考查 ( )作为本刊 1 0 ( 2 )的续篇 ,含 2 6科约 1 2 6种。(四十三 )小蠹科 Scolytidae1 6 5.瘤胸材小蠹 Ambrosiodusrubricollis( Eichhoff) [1 4、1 7] 分布 :建阳、建瓯。 (黄建采集 ,黄复生鉴定 )1 6 6 .削尾材小蠹 H adrodemius mutilatus ( Blandford) [1 4 ] 分布 :将乐龙栖山。1 6 7.小咪小蠹 H ypothenemus eruditus Westwood[1 4 ] 分布 :福建。1 6 8.小滑材小蠹 Xylosandrus compactus Eichhoff[1 4…     

北海道黄杨树的组织培养

1　植物名称　北海道黄杨树 (Euonymusjaponicuscv.Zhuzi) [1 ] 。2　材料类别　成年植株带腋芽的茎段 (caulineseg ment)。3　培养条件　培养基有 :( 1 )MS +NAA 0 .2mg·L- 1 (单位下同 ) + 6 BA 2 .0 ;( 2 )MS +NAA 0 .1 + 6 BA 1 .0 ;( 3)MS +NAA 0 .0 5 + 6 BA 0 .5 ;( 4 )MS +NAA 0 .1 + 6 BA 0 .5 ;( 5 )MS +NAA 0 .1 + 6 BA 1 .0 ;( 6) 1 /2MS +NAA 0 .5 + 6 BA 0 .1。以上培养基含 3%蔗糖、0 .8%琼脂 ,pH 5 .8。培养温度为 ( 2 1±3)℃ ,光照度为 1 5 0 0lx ,光照时间为 1 2h·d- 1 。4　生长与分化情况4.1　无…     

金铁锁的新三萜皂甙

从金铁锁（Psammosilene tunicoides W.C.Wu et C.Y.Wu)根部分离得到5个齐墩果烷型五环三萜皂苷,它们的结构通过波谱和化学方法分别鉴定为：3-O-β-D-galactopyranosyl-(1→2)-β-D-glucuronopyranosyl-gypsogenin(1),3-O-β-D-galactopyranosyl-(1→2)-[β-D-galactopyranosyl-(1→3)-β-D-glucuronopyranosyl-gypsogenin(2),3-O-β-D-galactopyranosyl-(1→2)-β-D-glucuronopyra-nosyl-gypsogenin-28-O-β-D-xylopyranosyl-(1→4)-[β-D-glucopyranosyl-(1→3)]-α-L-rhamnopyranosyl(1→2)-β-D-fucopyranoside(LobatosideI,3),3-O-β-D-galactopyranosyl-(1→2)-[β-D-xylopyranosyl-(1→3)-β-D-glucuronopyranosylgypsogenin-28-O-β-D-xylopyranosyl-(1→4)-[β-D-glucopyranosyl-(1→3)]-α-L-rhamnopyranosyl(1→2)-β-D-fucopyranoside(4),3-O-β-D-galactopyranosyl-(1→）-β-D-glucuro-nopyranosyl-grpsogenin-28-O-β-D-xylopyranosyl-(1→4)-[β-D-6-O-acetylglucopyranosyl-(1→3)-β-D-glucuro-nopyranosyl-gypsogenin-28-O-β-D-xylopyranosyl-(1→4)-[β-D-6-O-acetylglucopyranosyl-(1→3)]-α-L-rh-amnopyranosyl(1→2)-β-D-fucopyranoside(5),其中5为新化合物,1和2为首次从自然界中分离得到。     

脂质体介导基因编辑载体质粒转染条件的优化

[目的]探讨脂质体介导基因编辑载体质粒转染人食管癌Eca-109细胞的最佳条件。[方法]以基于Cre/Lox P系统的p GT-A1B1和基于CRISPR/Cas9系统的p X458-sgRNA8两种基因编辑载体质粒为实验材料,将环状和线性质粒以不同DNA用量(0. 2、0. 4、0. 6和0. 8μg)和不同DNA与脂质体比例(1∶1、1∶1. 5、1∶2、1∶2. 5和1∶3)转染Eca-109细胞,计算转染效率。[结果]不同DNA用量条件下,p GT-A1B1在0. 4μg和0. 6μg时转染效率较高,p X458-sgRNA8在0. 6μg时转染效率较高,与其它DNA用量比较均有显著性差异(P 0. 05)。不同DNA与脂质体比例条件下,p GT-A1B1在比例为1∶1. 5和1∶2时转染效率较高,p X458-sgRNA8在比例为1∶2. 5时转染效率较高,与其它比例比较均有显著性差异(P 0. 05)。同一种质粒的环状和线性结构形态,在DNA用量或DNA与脂质体比例相同时,转染效率差异不显著(P 0. 05)。[结论]建立了脂质体介导基因编辑载体质粒转染Eca-109细胞的最佳转染条件,质粒p GT-A1B1和p X458-sgRNA8的DNA用量分别为0. 4～0. 6μg和0. 6μg,DNA与脂质体比例分别为1∶1. 5～1∶2和1∶2. 5。     

山葵未成熟胚离体培养和植株再生

1　植物名称　山葵 (Ｅｕｔｒｅｍａｗａｓａｂｉ)日本品种岛根 3号。2　材料类别　开花 2 0ｄ后的荚果中剥出的未成熟种子 (种皮 未成熟胚 )。3　培养条件　基本培养基为自行设计的“贵山”(代号ＧＳ)配方[1 ] 。 ( 1 )诱导愈伤组织培养基为 :ＧＳ 6 ＢＡ 0 .1ｍｇ·Ｌ- 1 (单位下同 ) 2 ,4 Ｄ 1 ;( 2 )芽分化培养基为 :ＧＳ 6 ＢＡ 0 .5 ＺＴ 0 .5 ＩＢＡ0 .0 1 ;( 3)芽增殖培养基为 :ＧＳ 6 ＢＡ 0 .4;( 4 )生根培养基为 :ＧＳ ＩＢＡ 0 .1 ＮＡＡ 0 .1。以上培养基均含 3%蔗糖 [( 1 )含 2 % ]和 0 .6%琼脂粉 ,ｐＨ5 .8～ 5…     

仁用杏的组织培养与快速繁殖

1　植物名称　杏 (Prunusarmeniaca)品种仁用杏“龙王帽”。2　材料类别　休眠芽 (dormantbud)。3　培养条件　芽启动分化培养基 (buddifferentia tonmedium) :( 1 )MS + 6 BA 0 .5mg·L- 1 (单位下同 ) ;( 2 )MS + 6 BA 0 .5 +IBA 0 .1 ;( 3)WPM +6 BA 0 .5 ;( 4 )WPM + 6 BA 0 .5 +IBA 0 .1。增殖培养基 (budmultiplicationmedium) :( 5 )WPM + 6 BA 1 .0 +IBA 0 .5 ;( 6)WPM + 6 BA 1 .0 +IBA 0 .5+GA33 ;( 7)MS + 6 BA 1 .0 +IBA 0 .2 ;( 8)NN69+ 6 BA 0 .5 +IBA 0 .1 ;( 9)NN69+ 6 BA 1 .0 +IBA 0 .2。生根…     

sIL—16结构与功能研究进展

1 .ｓＩＬ 1 6的来源与结构白细胞介素 1 6(ｉｎｔｅｒｌｅｕｋｉｎ 1 6,ＩＬ 1 6) ,又名淋巴细胞趋化因子 (ｌｙｍｐｈｏｃｙｔｅｃｈｒｏ ｍａｔａｘｉｓｆａｃｔｏｒ ,ＬＣＦ) ,是 1 982年由ＣｒｕｉｋＳｈａｎｋ实验室从抗原刺激的单核细胞中分离提纯的[1] ,主要来源于外周血单核细胞 ,它的前体由 63 1个氨基酸构成 ,无生物学活性 ,被白介素 1 β 转化酶 (ｃａｓｐａｓｅ 3 ,ｉｎｔｅｒｌｅｕｋｉｎ 1 β ｃｏｎ ｖｅｒｔｉｎｇｅｎｚｙｍｅＩＣＥ/ＣＥＤ 3 ｐｒｏｔｅａｓｅ)在Ａｓｐ5 10 和Ｓｅｒ5 11位酶切后[2 ] ,形成 1 2 1个氨基…     

长翅秋海棠的叶片培养和快速繁殖

1　植物名称　长翅秋海棠 (Ｂｅｇｏｎｉａｌｏｎ ｇｉａｌａｔａ)。2　材料类别　初展幼叶。3　培养条件　不定芽诱导培养基和增殖培养基分别采用 :( 1 )ＭＳ ＮＡＡ 0 .5ｍｇ·Ｌ-1(单位下同 ) 6 ＢＡ 1 ;( 2 )ＭＳ ＩＡＡ 0 .5 6 ＢＡ 1 ;( 3)ＭＳ ＮＡＡ 1 6 ＢＡ 0 .5 ;( 4 )ＭＳ ＮＡＡ 1 6 ＢＡ 1 .5。根的诱导采用 :( 5 ) 1 /2ＭＳ ＩＢＡ 1 ;( 6 ) 1 /2ＭＳ ＮＡＡ 1。以上培养基均加入 0 .6 %琼脂粉 ,ｐＨ 5 .8。( 1 )、( 2 )、( 3)、( 4 )分别加入 3%蔗糖 ,( 5 )、( 6 )分别加入 1 .5 %蔗糖。培养温度 ( 2 5±3)℃…     

罗汉果化学成分的研究

用硅胶柱层析、制备薄层层析和Sephadex LH-20柱层析等方法对罗汉果[Siraitia grosvenorii(Swingle)C.Jeffrey]75%乙醇提取物化学成分进行分析,共分离得到8个化合物,通过质谱法和核磁共振波谱法及理化性质鉴定为:罗汉果醇苯甲酸酯(1)、厚朴酚(2)、双[5-甲酰基糠基]醚(3)、5-羟甲基糠酸(4)、山柰酚-7-O-α-L-鼠李糖苷(5)、山柰酚-3,7-O-α-L-二鼠李糖苷(6)、山柰酚(7)、琥珀酸(8).除化合物1、6和7外,其余均为首次从该植物中分离得到.     

狭基线纹香茶菜中一个新的木脂素类化合物(英文)

从狭基线纹香茶菜 (Isodonlophanthoidesvar.gerardianus [Bentham]H .Hara)的乙酸乙酯部分分离得到两个木脂素类化合物 ,经 1D、2D_NMR技术鉴定 ,分别为 1_acetoxyl_2e,6e_dipiperonyl_3,7_dioxabicyclo_[3,3,0 ]_octane (1)和 1_acetoxyl_2e_piperonyl_6e_[6_methoxyl_piperonyl]_3,7_dioxabicyclo_[3,3,0 ]_octane (2 ) ,其中 2为新化合物。     

Binding of the bioactive component jatrorrhizine to human serum albumin

The interaction between Jatrorrhizine with human serum albumin (HSA) were studied by fluorescence quenching technique, circular dichroism (CD) spectroscopy, and Fourier transform infrared (FT-IR) spectroscopy. Fluorescence data revealed the presence of a single class of binding site on HSA and its binding constants (K) are 7.278 x 10(4), 6.526 x 10(4), and 5.965 x 10(4) L.mol(-1) at 296, 303, and 310 K, respectively. The CD spectra and FT-IR spectra have proved that the protein secondary structure changed in the presence of Jatrorrhizine in aqueous solution. The effect of common ions on the binding constants was also investigated. In addition, the thermodynamic functions standard enthalpy (DeltaH(0)) and standard entropy (DeltaS(0)) for the reaction were calculated to be -10.891 kJ.mol(-1) and 56.267 J.mol(-1) K(-1), according to the van't Hoff equation. These data indicated that hydrophobic and electrostatic interactions played a major role in the binding of Jatrorrhizine to HSA. Furthermore, the displacement experiments indicated that Jatrorrhizine could bind to the site I of HSA, which was also in agreement with the result of the molecular modeling study.     

胡椒碱分子键合人血清白蛋白位点的表征

利用荧光光谱法、紫外光谱法并结合计算机模拟技术在分子水平上研究了胡椒碱与人血清白蛋白(human serum albumin HSA)的键合作用.同步荧光及紫外光谱图表明,胡椒碱对HSA微环境有影响.位点竞争试验证明,胡椒碱分子键合在HSA的位点Ⅱ区.通过荧光光谱滴定数据求得不同温度下(300K 310K和318 K)药物与蛋白相互作用的结合常数及结合位点数.分子模拟的结果显示了胡椒碱与HSA的键合区域和键合模式,表明药物与蛋白有较强的键合作用;维持药物与蛋白质的相互作用力主要是疏水用,兼有氢键(位于氨基酸残基Arg 257,Arg 222及Arg218位).通过实验数据计算得到的热力学参数(ΔH0与ΔS0的值分别为原33.11 kJ·mol-1和原18.90 J·mol原1·K-1)确定了胡椒碱与HSA分子的相互作用力类型主要为氢键兼范德华力.     

Interaction of rhein with human serum albumin investigation by optical spectroscopic technique and modeling studies

The binding of rhein with human serum albumin (HSA) has been studied in detail by spectroscopic method including circular dichroism (CD), Fourier transformation infrared spectra (FT-IR), fluorescence spectra. The binding parameters for the reaction have been calculated according to Scatchard equation at different temperatures. The plots indicated that the binding of HSA to rhein at 303, 310 and 318 K is characterized by one binding site with the affinity constant K at (4.93+/-0.16)x10(5), (4.02+/-0.16)x10(5) and (2.69+/-0.16)x10(5) M-1, respectively. The secondary structure compositions of free HSA and its rhein complexes were estimated by the FT-IR spectra. FT-IR and curve-fitted results of amide I band are in good agreement with the analyses of CD spectra. Molecular Modeling method was used to calculate the interaction modes between the drug and HSA.     

Toxic effects of chrysoidine on human serum albumin: isothermal titration calorimetry and spectroscopic investigations

Chrysoidine is widely used in industry as a type of azo dye, and is sometimes used illegally as a food additive despite its potential toxicity. Human serum albumin (HSA) is one of the most important proteins in blood plasma and possesses major physiological functions. In the present study, the conformational and functional effects of chrysoidine on HSA were investigated by isothermal titration calorimetry (ITC), multiple spectroscopic methods, a molecular docking study and an esterase activity assay. Based on the ITC results, the binding stoichiometry of chrysoidine to HSA was estimated to be 1.5:1, and was a spontaneous process via a single hydrogen bond. The binding of chrysoidine to HSA induced dynamic quenching in fluorescence, and changes in secondary structure and in the microenvironment of the Trp‐214 residue. In addition, the hydrogen bond (1.80 Å) formed between the chrysoidine molecule and the Gln‐211 residue. The esterase activity of HSA decreased following the addition chrysoidine due to the change in protein structure. This study details the direct interaction between chrysoidine and HSA at the molecular level and the mechanism for toxicity as a result of the functional changes induced by HSA structural variation upon binding to chrysoidine in vitro. This study provides useful information towards detailing the transportation mechanism and toxicity of chrysoidine in vivo. Copyright © 2015 John Wiley & Sons, Ltd.     

Probing the interaction of anticancer drug temsirolimus with human serum albumin: molecular docking and spectroscopic insight

The binding interaction between temsirolimus, an important antirenal cancer drug, and HSA, an important carrier protein was scrutinized making use of UV and fluorescence spectroscopy. Hyper chromaticity observed in UV spectroscopy in the presence of temsirolimus as compared to free HSA suggests the formation of complex between HSA and temsirolimus. Fluorescence quenching experiments clearly showed quenching in the fluorescence of HSA in the presence of temsirolimus confirming the complex formation and also confirmed that static mode of interaction is operative for this binding process. Binding constant values obtained through UV and fluorescence spectroscopy reveal strong interaction; temsirolimus binds to HSA at 298 K with a binding constant of 2.9 × 10⁴ M^?1implying the strength of interaction. The negative Gibbs free energy obtained through Isothermal titration calorimetry as well as quenching experiments suggests that binding process is spontaneous. Molecular docking further provides an insight of various residues that are involved in this binding process; showing the binding energy to be -12.9 kcal/mol. CD spectroscopy was retorted to analyze changes in secondary structure of HSA; increased intensity in presence of temsirolimus showing changes in secondary structure of HSA induced by temsirolimus. This study is of importance as it provides an insight into the binding mechanism of an important antirenal cancer drug with an important carrier protein. Once temsirolimus binds to HSA, it changes conformation of HSA which in turn can alter the functionality of this important carrier protein and this altered functionality of HSA can be highlighted in variety of diseases.     

DNA interaction with human serum albumin studied by affinity capillary electrophoresis and FTIR spectroscopy

The question addressed in this study is how does the protein-DNA complexation affect the structure and dynamics of DNA and protein in aqueous solution. We examined the interaction of calf-thymus DNA with human serum albumin (HSA) in aqueous solution at physiological conditions, using constant DNA concentration of 12.5 mM (phosphate) and various HSA contents 0.25 to 2% or 0.04 to 0.3 mM. Affinity capillary electrophoresis and FTIR spectroscopic methods were used to determine the protein binding mode, the association constant, sequence preference, and the biopolymer secondary structural changes in the HSA-DNA complexes. Spectroscopic evidence showed two types of HSA-DNA complexes with strong binding of K(1) = 4.5 x 10(5) M(-1) and weak binding of K(2) = 6.10 x 10(4) M(-1). The two major binding sites were located on the G-C bases and the backbone PO(2) group. The protein-DNA interaction stabilizes the HSA secondary structure. A minor alteration of B-DNA structure was observed, while no major protein conformational changes occurred.     

Interaction of isofraxidin with human serum albumin

This study was designed to examine the interaction of isofraxidin with human serum albumin (HSA) under physiological conditions with drug concentrations in the range of 3.3 x 10(-6) mol L(-1)-3.0x10(-5) mol L(-1) and HSA concentration at 1.5 x 10(-6) mol L(-1). Fluorescence quenching methods in combination with Fourier transform infrared (FT-IR) spectroscopy and circular dichroism (CD) spectroscopy were used to determine the drug-binding mode, the binding constant and the protein structure changes in the presence of isofraxidin in aqueous solution. Spectroscopic evidence showed that the interaction results in one type of isofraxidin-HSA complex with binding constants of 4.1266 x 10(5) L mol(-1), 3.8612 x 10(5) L mol(-1), 3.5063 x 10(5) L mol(-1), 3.1241 x 10(5) L mol(-1) at 296 K, 303 K, 310 K, 318 K, respectively. The thermodynamic parameters, enthalpy change (DeltaH) and entropy change (DeltaS) were calculated to be -10.08 kJ mol(-1) and 73.57 J mol(-1) K(-1) according to van't Hoff equation, which indicated that hydrophobic interaction played a main role in the binding of isofraxidin to HSA. The experiment results are nearly in accordance with the calculation results obtained by Silicon Graphics Ocatane2 workstation.     

Multi-spectroscopic and molecular modelling approach to investigate the interaction of riboflavin with human serum albumin

Riboflavin (RF) plays an important role in various metabolic redox reactions in the form of flavin adenine dinucleotide and flavin mononucleotide. Human serum albumin (HSA) is an important protein involved in the transportation of drugs, hormones, fatty acid and other molecules which determine the biodistribution and physiological fate of these molecules. In this study, we have investigated the interaction of riboflavin RF with HSA under simulative physiological conditions using various biophysical, calorimetric and molecular docking techniques. Results demonstrate the formation of riboflavin–HSA complex with binding constant in the order of 10⁴ M^?1. Fluorescence spectroscopy confirms intermediate strength having a static mode of quenching with stoichiometry of 1:1. Experimental results suggest that the binding site of riboflavin mainly resides in sub-domain IIA of HSA and that ligand interaction increases the α-helical content of HSA. These parameters were further verified by isothermal titration calorimetry ITC which confirms the thermodynamic parameters obtained by fluorescence spectroscopy. Molecular docking was employed to suggest a binding model. Based on thermodynamic, spectroscopic and computational observations it can be concluded that HSA-riboflavin complex is mainly stabilized by various non-covalent forces with binding energy of ?7.2 kcal mol^?1.     

Binding of the bioactive compound 5,7,4'-trihydroxy-6,3',5'-trimethoxyflavone to human serum albumin

5,7,4'-trihydroxy-6,3',5'-trimethoxyflavone is one of the bioactive components isolated from Artemisia plants possessing antitumor therapeutic activities. In this paper, its binding properties and binding sites located on human serum albumin (HSA) have been studied using UV absorption spectroscopy, fluorescence spectroscopy and Fourier transform infrared (FT-IR) spectra. The results of fluorescence titration revealed that 5,7,4'-trihydroxy-6,3',5'-trimethoxyflavone could strongly quench the intrinsic fluorescence of HSA by static quenching and there was only one class of binding sites on HSA for this drug. The binding constants at four different temperatures (289, 298, 310, and 318 K) were 1.93, 1.56, 1.22, and 0.93x10(5) L mol-1, respectively. The FT-IR spectra evidence showed that the protein secondary structure changed with reduction of alpha-helices about 27.6% at the drug to protein molar ratio of 3. The thermodynamic functions standard enthalpy change (DeltaH0) and standard entropy change (DeltaS0) for the reaction were calculated to be -18.70 kJ mol-1 and 36.62 J mol-1 K-1 according to the van't Hoff equation. These results and the molecular modeling study suggested that hydrophobic interaction was the predominant intermolecular force stabilizing the complex, and 5,7,4'-trihydroxy-6,3',5'-trimethoxyflavone could bind to the site I of HSA (the Warfarin Binding site).     

Spectroscopic and thermodynamic determination of three distinct binding sites for Co(II) ions in human serum albumin

Human serum albumin (HSA) is the most abundant protein of blood serum, involved in the transport of metal ions, including Co(II). Using circular dichroism spectroscopic titrations we characterized three distinct Co(II) binding sites in HSA. Applying Cu(II), Ni(II) and Cd(II) ions as competitors we determined that these sites are identical with three binding sites known for other metal ions. We ordered these sites according to their binding affinities as cadmium site B (CdB) > multi-metal binding site (MBS) > N-terminal binding site (NTS). Using isothermal titration calorimetry (ITC) we confirmed the presence of these three binding sites and determined their conditional binding constants at pH 7.4 as 9 ± 5, 1.1 ± 0.5, and 0.9 ± 0.3 × 10⁴ M⁻¹, respectively. The impact of these results on the albumin cobalt binding (ACB) clinical assay for myocardial ischemia is discussed.