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trishcl
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  tris-hcl
     In pH=8. 5 Tris-HCl medium. the electrode has a linear response in the range of 5. 0 × 10-5-1. 10×10-3 mol/L of alcohol.
     在 pH 8. 5的 Tris-HCl介质中,该传感器的响应电流与乙醇浓度在 5. 0× 10-5~ 1.10×10-3mol/L范围内有良好的线性关系。
短句来源
     Diets madeby 0. 01 mol . L- 1 Tris-HCl buffer , pH 8. 0 and 0. 01 mol . L-1 glycine-NaOH buffer, pH 10. 0, all sig-nificantly increased the toxicity of crystals and no difference between them was observed.
     以pH为8.0的0.01mol·L-1Tris-HCl缓冲液及pH为10.0的0.01mol.L-1glycine-NaOH缓冲液配制饲料,晶体的毒力显著增高。
短句来源
     Omphalia lapideacens lectin (OLL) has been purified by extraction with Tris-HCl buffer,anunonium sulfate frachonation, ion-exchange column, and affinity chromatograPhy on an ovomucoid-Sepharose 4B column and Sephacryl-S100 column.
     雷丸(OmphalialapidescensSchroct.)经过Tris-HCl缓冲液浸提,硫酸铵分级沉淀,离子交换,卵粘蛋白-Sepharose4B亲和层析以及Sephacryl-S100分子筛等步骤,纯化得到纯度为95%以上的雷扎凝集素(简称OLL)。
短句来源
     In Tris-HCl (PH=7.4) buffer (25ml, 37.0±0.1℃), its daily in vitro release was assayed by UV spectrophotometry at 295nm. The release Profile showed this drug rod released without any initial burst.
     体外释放在Tris-HCl(PH7.4)缓冲溶液介质中,温度为37±0.1℃时,其释放初期的释药量为其膜剂的近1/30,能较好地控制释药初期的“爆释”现象。
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     The binding field between the cow serum albumin and the bilirubin was studied by paper chromatography. The interaction forces of the cow serum albumin and egg albumin with the bilirubin were compared with the visible absorption spectrocopy in buffer solution of KH 2PO 4 and Tris-HCl.
     本文利用纸上色谱法研究了牛血清白蛋白分子与胆红素作用的结合物,同时利用可见吸收光谱法比较了牛血清白蛋白分子和鸡蛋清白蛋白分子分别在KH2PO4缓冲液和Tris-HCl缓冲液中与胆红素的作用力。
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  tris hcl
     In addition,the effects of three kinds of buffers on ALD activity were also evaluated,including TEA HCl(pH8 0),Tris HCl(8.0),and Collidine HCl(pH7 5). The results indicated that ALD activity was highest in TEA buffer;
     本文对TEA-HCl(pH8.0)、Tris-HCl(pH8.0)和Colidine-HCl(pH7.5)三种缓冲液用于ALD活性测定效果进行了评价,结果表明在TEA缓冲液中所测ALD活性最高;
短句来源
     The optimum testing condi tions of the lactate enzyme electrode are as follows 0 025 mol·L -1 Tris HCl buffer at pH8 5 and 25 ℃. The buffer contained 1 5 mmol·L -1 Vi twmik k 3 as electron mediator.
     此乳酸盐酶电极测试的最优条件是:在pH85的Tris-HCl缓冲液中进行,温度25℃,此缓冲液中含15mmol·L-1Vk3电子介体。
短句来源
     The purified enzyme after concentrated is stored without a loss of activity for a month at -20℃ in the dark in the 0.1 mol·L -1 Tris HCl buffer,pH 8.5,including 50% glycerol 5 mmol·L -1 2 mercaptoethanol and MgCl 2.
     纯化的ALAD浓缩后,- 20℃下在0.1 m ol·L- 1,pH 8.5 的Tris-HCl,内含50% 的甘油,5 m m ol·L- 1的巯基乙醇和MgCl2 中黑暗贮藏30 d 酶活不损失
短句来源
     The analytical column was 35mm×4.6mm i.d. TSK del DEAE NPR, 2 5μm of which the surface was chemically bonded with diethylaminoethyl groups. pBR322 DNA Hae Ⅲ digest, Lambda DNA Hind Ⅲ digest and a kind of PCR product have been separated by gradient elution of sodium chloride in 20mmol/L Tris HCl buffer(pH 9.0).
     建立了高效液相色谱非多孔型阴离子交换柱分离DNA片段的方法,用TSKgelDEAE-NPR柱、Tris-HCl缓冲液(pH9.0)、1.0mol/LNaCl多阶式线性梯度洗脱,分析了核酸分子量参照物pBR322DNA-HaeⅢ,LambdaDNA-HindⅢ及乙肝病毒基因PCR产物,探讨了梯度、流速对分离的影响,方法简便、快速、分辨率高
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  “tris-hcl”译为未确定词的双语例句
     The regulatory action of endogenous inorganic phosphate in the chloroplasts on Mg2+-ATPase function wasstudied. The endogenous inorganicphosphate content in chloroplasts decreased markedly after washing withSTN (sucrose, 0. 4 mol/L; NaCI,0. 01 mol/L and Tris-HCI, 0. 02 mol/L, pH 7. 4) buffer. This decrease inhibited the Mg2+-ATPase activitymarkedly (Table 1, 2).
     用STN(含蔗糖,0.4mol/L;NaCl,0.01mol/L和Tris-HCl,0.02mol/L,pH7.4)提取的菠菜叶片叶绿体再用STN洗涤后,它的内源无机磷酸盐含量急剧减少,其Mg2+-ATP酶水解ATP的能力明显下降。
短句来源
     (2)The optimal measurement conditions might be described as follows: 20μl sample was first incubated in 2.0ml, pH 8.2,0.1mol/L TrisHCl buffer at 25°C for 2min,then 0.2mol/L pyrogallic acid was added in 20μl (the final concentration was 10mmol/L);
     ②最佳测试条件为:在25℃时,0.1mol/L,pH8.2的Tris-HCL缓冲液0.2ml,样品用量5~20μl,0.2mol/L焦性没食子酸加入量为20μl(终浓度10mmol/L);
短句来源
     Results (1)The order of impact of several factors on assay was as follows: pH of TrisHCl buffer>the concentration or the volume of pyrogallic acid>the volume of TrisHCl buffer>the concentration of TrisHCl buffer>stirring speed;
     结果①影响测试结果的因素依次为:Tris-HCL缓冲液的pH值>焦性没食子酸浓度>Tris-HCL缓冲液的体积>Tris-HCL缓冲液的浓度>搅拌速度;
短句来源
     finally, the oocysts were strilized by incubating in 5 % cold NaOCl for 10min. After prepared crude material, the sporozoites and second generation merozoites were further purified by DEAE-cellulose 52 anion exchange chromatography with 0. 05 mol .
     孢子化卵囊经研磨,消化,游离出子孢子后,过DEAE-纤维素52层析柱,以0.05mol·mL-1,Tris-HCl,(pH=80,0.15mol·mL1-NaCl)洗脱,层析往高5cm,洗脱液水柱高3cm,流速为2mL·min-1,纯化出了子孢子。
短句来源
     The limited substrate was starch calibrated with appointed starch, the wavelength was 700 nm or 800 nm, the result was reported with PNPG 7 limited substrate enzymatic activity.
     底物浓度改为0.79g/L,底物缓冲液以Tris-HCl(pH7.0,37℃,50mmol/L)为缓冲剂,并加入2.5mmol/LCaCl2和100mmol/LNaCl以保证对α-AMS的激活作用,酶促反应时间选为5min,测定波长选定为700(或800/700)nm。
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  trishcl
GroEL labeled in 50mM TrisHCl, pH 7.8, incorporated ~0.3 labels each on C138 and C458.
      
The emf was recorded for equimolal bis-tris/bis- trisHCl buffer solutions from 5 to 125°C at approximately 25°C intervals, and at nine ionic strengths from 0.05 to 5.0m (NaCl).
      
After 12 h at 55 C, the extract was purified using TrisHCl-saturated buffered phenol and a chloroform/isoamyl solution.
      
All Abs were diluted to the appropriate concentration in TrisHCl pH 7.5 with 0.1% Tween-20 and 0.1% sodium azide.
      
Column fractions were immediately neutralised and dialysed against 10 mM TrisHCl, pH 7.5.
      
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The studies of affectors affecting RAPD were carried out by the 12 species of CLanatus as template DNAThe results showed that the purification of template DNA,the concentrations of template DNA,Taq polymerase,random primer,Mg2+and the PCR programe played an important role in RAPD analysisBased on the researches above,a technical system for RAPD analysis in species of Clanatus was established:in 10 L reaction solution,containing 10 ng/10 L template DNA,05 mol/L random primer,50 mmol/L TrisHCl(pH83),500...

The studies of affectors affecting RAPD were carried out by the 12 species of CLanatus as template DNAThe results showed that the purification of template DNA,the concentrations of template DNA,Taq polymerase,random primer,Mg2+and the PCR programe played an important role in RAPD analysisBased on the researches above,a technical system for RAPD analysis in species of Clanatus was established:in 10 L reaction solution,containing 10 ng/10 L template DNA,05 mol/L random primer,50 mmol/L TrisHCl(pH83),500 g/mL BSA,25 mmol/L MgCl2,06 U/10 L Taq DNA,200 mol/L dNTPs

以西瓜种内的12个品种(系)为模板DNA,研究了影响RAPD扩增效果的因素。结果表明,模板DNA、Taq酶、随机引物、Mg2+浓度以及PCR反应程序在RAPD分析中都具有重要的作用。根据以上因子的研究结果,建立了适合西瓜种植物的RAPD分析的技术体系:10μL反应液中,模板10ng/10μL,引物05μmol/L,TrisHCl(pH83)50mmol/L,BSA500μg/mL,MgCl225mmol/L,TaqDNA06U/10μL,dNTPs200μmol/L,10%蔗糖400和1mmol/L甲酚红。

Contraceptive levonorgestrel (LNG) was coupled to polyα、β(3hydroxypropyl)DLaspartamide,a biodegradable and biocompatible material.The drug loaded in the polymer was about 27.0% (w/w). The polymer conjugate was characterized by differential scanning calorimertry (DSC) and fourier transform infrared (FTIR). The in vitro release of levonorgestrel from the biocompatible polymer conjugate was studied in TrisHCl (0.1 mol/L) and trypsin. Levonorgertrel was measured by HPLC. The data indicate that this levonorgestrel...

Contraceptive levonorgestrel (LNG) was coupled to polyα、β(3hydroxypropyl)DLaspartamide,a biodegradable and biocompatible material.The drug loaded in the polymer was about 27.0% (w/w). The polymer conjugate was characterized by differential scanning calorimertry (DSC) and fourier transform infrared (FTIR). The in vitro release of levonorgestrel from the biocompatible polymer conjugate was studied in TrisHCl (0.1 mol/L) and trypsin. Levonorgertrel was measured by HPLC. The data indicate that this levonorgestrel polymer conjugate can be released in these two systems but faster in trypsin.$

具有临床意义的甾体类避孕药左旋 1 8甲基炔诺酮 (L NG)键合于生物相容性聚氨基酸材料 :α、β 聚 (3羟丙基 ) DL 天冬酰胺上 ,制成长效控释药物。用红外光谱法、差热分析等分别对材料及键合药物进行了表征 ,药物的接入率达 2 7.0 % (w/ w) (n=3) ,共价缩合物以棒状形式释药进行了体外水解和酶解释放试验。结果表明 ,酶解释放比水解释放略快

A proteinase,which has important work on turbot digestive,was purified from turbot(Scophthalmus maximus L.) and its major physical and chemical characteristics were studied and reported in this article.The intestine proteinase extraction was prepared through homogenate and centrifugation by Tris-HCl buffer at low temperature.The supernatant was purified through ammonium sulfate grading precipitation further and the active component was dialyzed and concentrated.Then the condensed proteinase was purified by means...

A proteinase,which has important work on turbot digestive,was purified from turbot(Scophthalmus maximus L.) and its major physical and chemical characteristics were studied and reported in this article.The intestine proteinase extraction was prepared through homogenate and centrifugation by Tris-HCl buffer at low temperature.The supernatant was purified through ammonium sulfate grading precipitation further and the active component was dialyzed and concentrated.Then the condensed proteinase was purified by means of DEAE-Sepharose Fast Flow anion-exchange chromatography with an elution of a linear gradient of 5 mmol·L~(-1) Tris-HCl buffer(pH 8.5) containing 1.0 mol·L~(-1) NaCl.At last,the pure enzyme was obtained through Sephadex G-100 chromatography with an elution of 5mmol·L~(1) TrisHCl buffer(pH 8.5).The purity of the purified intestine proteinase was confirmed by the presence of a single band on SDS-PAGE.The relative molecular mass of this enzyme was determined to be about 58 kD.By using casein as substrate to measure proteinase activity,the characterization of turbot intestine proteinase was made.The enzyme is stable at pH 6.0-11.0 and temperature below 30 ℃.When the temperature rose,there was a rapid decline of its stability.The enzyme showed maximum activity at pH 9.0 and 50 ℃.When the temperature declined,the optimum pH of enzyme showed a trend of moving to alkaline.And when the action time prolonged,the optimum temperature of enzyme showed a trend to decline.Furthermore,the enzyme is activated by Mn~(2+) and inactivated by Cu~(2+),Zn~(2+),Ag~+,Fe~(3+).In further studies,it was inhibited by SH-enzyme inhibitors such as p-Hydroxymercuribenzoate(PCMB) and N-bromosuccinimide(NBS) remarkably,and partially inhibited by tosyl-lysine chloromethyl ketone(TLCK).Using casein as the substrate, the Km value of enzyme is 2.92 g·L~(-1) at pH 9.0,50 ℃.The result showed the enzyme seemed to be a SH-enzyme.

以大菱鲆肠道为材料,对大菱鲆消化生理中起重要作用的肠蛋白酶的分离纯化条件和理化性质进行了研究。经Tris-HCl缓冲液抽提,硫酸铵分级分离,DEAE-Sepharose Fast Flow离子交换层析、Sephadex G-100凝胶过滤层析分离纯化,获得大菱鲆肠蛋白酶Ⅰ的电泳纯制品,并对该酶的性质进行了研究。结果显示:纯酶的分子量约为58kD。纯酶最适反应pH为9.0,最适反应温度50℃;pH稳定范围6.0~11.0,30℃以下酶活性稳定;Mn2+可激活大菱鲆肠蛋白酶Ⅰ,Cu2+、Zn2+、Ag+、Fe3+则对酶活性有抑制作用;巯基蛋白酶抑制剂显著抑制大菱鲆肠蛋白酶Ⅰ的活性,金属蛋白酶抑制剂对大菱鲆肠蛋白酶Ⅰ无影响。50℃、pH9.0条件下以双倒数作图法得大菱鲆肠蛋白酶Ⅰ催化酪蛋白水解的Km值为2.92g.L-1。

 
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