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tris base
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  “tris base”译为未确定词的双语例句
     Molar enthalpy (?Hm,1) of the enzymatic reaction was determined to be 0.63 kJ? mol-1 by deducting enthalpy of protonization of Tris base from total enthalpy of reaction system.
     通过测量实验条件下反应体系的总反应焓及相同条件下的Tris碱的质子化焓,确定了酶反应的摩尔反应焓ΔHm,1为0.63kJ?
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  相似匹配句对
     Base on J.
     本文从J.
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     Base on the C.
     根据C.
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     campes-tris pv.
     pv.
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     Preparation of tris-adenosine triphosphate
     腺苷三磷酸-三羟甲基氨基甲烷(Tris-ATP)的制备
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  tris base
Unbound dye is removed by a series of four 2.5 min washes in 1% acetic acid, and protein-bound dye extracted with 10 mM unbuffered Tris base for spectrophotometric optical density determination at 433 nm.
      
When needed, Tris base was added to the samples to neutralize acidity.
      
Unbound dye was removed by washing four times with 1% acetic acid, and protein bound dye was extracted with 10 mM unbuffered Tris base.
      
The transfer buffer contained 15 mm Tris base, 120 mm glycine, and 5% methanol.
      
The rehydration was performed overnight in solubilization buffer without Tris-base according to manufacture's instructions.
      
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Proteomics is a challenging field that has been growing rapidly in the postgenomic era.Protein preparation is a key procedure for two-dimensional electrophoresis (2-DE) proteomics.In the current study,three procedures of protein sample preparation,namely basic,dialysis and acetone methods,were compared for establishment of an optimal method to extract proteins from rat bone,based on 2-DE maps from protein samples prepared by the three methods.Of the three methods,acetone method is the best one.Using this method...

Proteomics is a challenging field that has been growing rapidly in the postgenomic era.Protein preparation is a key procedure for two-dimensional electrophoresis (2-DE) proteomics.In the current study,three procedures of protein sample preparation,namely basic,dialysis and acetone methods,were compared for establishment of an optimal method to extract proteins from rat bone,based on 2-DE maps from protein samples prepared by the three methods.Of the three methods,acetone method is the best one.Using this method to purify proteins from rat bone,high quality of peptide mass fingerprint can be achieved.The procedure of the method is as follows.Prepared bone (1.0 g) was placed in an earthen bowl to grind into powder in liquid nitrogen and then 3 mL ice-cold buffer (1.44 g urea,0.46 g sulfocarbamide,0.12 g CHAPS,0.047 g DTT,0.015 g Tris-base,30 μL 100 mmol/L PMSF) was added to it.After stored at 4℃ overnight,these samples were centrifuged at 12 000 g for 30 min.The supernatant was dialyzed against 0.01 mol/L PBS for 24 h.Then ten times of volumes of cooled acetone were added to the specimen for the concentration of proteins.Followed by the store at -20℃ for 2 h,the proteins were obtained by centrifugation and then dry at 4℃.Before the isoelecric focusing,the sample was redissolved in the buffer (7 mol/L urea,4% CHAPS,100 mmol/L DTT,40 mmol/L Tris,2 mol/L sulfocarbamide,0.5% ampholyte (pH 5~7),1 mmol/L PMSF) at the room temperature for 2 h.The results may provide a valuable method of sample preparation for study of bone proteomics.

蛋白质组学是目前研究的重要热点.该文拟建立大鼠骨组织蛋白质样品提取的最佳方法,用于双向电泳分离,为进一步进行蛋白组学分析奠定基础.实验对3种不同方法制备的样本进行同一条件的二维电泳(2- DE)图谱,比较2- DE的结果.结果发现,丙酮沉淀法最佳.这些结果提示,只有结合骨组织成分特征与双向电泳的具体要求,选择恰当的样品提取液,采用合理的提取步骤,获得蛋白质样品,才能得到清晰高分辨率的电泳图谱,满足蛋白质组学分析需要.

Different protein extraction methods were comparatively examined with Lathyrus sativus leaves as the experimental material and on the basis of this the sample preparation was studied.The choices of IPG strips and the protocols,parameters and staining methods of the first phase IEF and the second-phase SDS-PAGE were compared and their conditions were optimized.The results showed that when TCA-acet precipitation was adopted to extract protein,Tris-base was added to the lysis solution as the protease...

Different protein extraction methods were comparatively examined with Lathyrus sativus leaves as the experimental material and on the basis of this the sample preparation was studied.The choices of IPG strips and the protocols,parameters and staining methods of the first phase IEF and the second-phase SDS-PAGE were compared and their conditions were optimized.The results showed that when TCA-acet precipitation was adopted to extract protein,Tris-base was added to the lysis solution as the protease inhibitor,when isoelectric focusing electrophoresis was adopted,the low voltage was prolonged(30 V,12 h;500 V,1 h;1 000 V,2 h)to help the salt ion electrophoresis and thus conduct the two-dimension electrophorsis of leaf protein of L.sativus,and when Coomassie brilliant blue and compound silver staining were adopted to stain the gel,the two dimension electrophoretograms with high reproduction and resolution power of leaf protein of L.sativus were obtained,wihich indicated that the optimized two-dimension electrophoresis of leaf protein of L.sativus was characterized with quality sample preparation and high electrophoresis resolution thus being completely suited to further proteomics research.

以山黧豆叶片为材料,比较分析了蛋白质的不同提取方法,在此基础上着重于样品制备.对IPG胶条的选择,第一向等电聚焦和第二向SDS-聚丙烯酰胺凝胶电泳的电泳程序及参数、染色方法等相关技术进行了比较和条件优化.结果显示:采用TCA-丙酮沉淀法提取蛋白质,裂解液中加入Tris-base作为蛋白酶抑制剂,等电聚焦电泳时延长低电压的电泳时间(30 V1、2 h,500 V1、h,1 000 V2、h)以促进盐离子泳出的方法对山黧豆叶片蛋白质进行双向电泳,并用考马斯亮蓝和银染复合染色法进行凝胶染色,能够获得蛋白点清晰的双向电泳图谱,说明用优化后的方法建立起的山黧豆叶片蛋白质双向电泳技术,蛋白质样品制备质量好,电泳分辨率高,完全适合于进一步的蛋白质组学研究.

At 37 ℃ and in Tris-HCl buffer (pH=7.4), enthalpy magnification technique and thermoki- netic initial rate method were employed to study the hydrolysis reaction of acetylcholine bromide catalyzed by acetylcholinesterase (AchE) and the inhibition of the reaction by sodium dodecyl sulfate (SDS) under near physiological conditions. Molar enthalpy (?Hm,1) of the enzymatic reaction was determined to be 0.63 kJ?mol-1 by deducting enthalpy of protonization of Tris base from total enthalpy of reaction system....

At 37 ℃ and in Tris-HCl buffer (pH=7.4), enthalpy magnification technique and thermoki- netic initial rate method were employed to study the hydrolysis reaction of acetylcholine bromide catalyzed by acetylcholinesterase (AchE) and the inhibition of the reaction by sodium dodecyl sulfate (SDS) under near physiological conditions. Molar enthalpy (?Hm,1) of the enzymatic reaction was determined to be 0.63 kJ?mol-1 by deducting enthalpy of protonization of Tris base from total enthalpy of reaction system. Micha- elis constant (Km) and substrate inhibition constant (KS) were also determined to be 0.85~0.94 mmol?L-1 and 0.74~0.83 mmol?L-1, respectively. SDS could remarkably decrease the rate of enzyme reaction but has less influence on biochemical constants of the enzyme. In SDS solution, inactivation rate of AchE follows first order reaction kinetics, the apparent first order inactivation constant is linear to action time and the fourth power of SDS concentration, and inactivation constant was calculated to be (2.47~2.69)×1013 mol-4?L4?min-1.

在37℃,pH=7.4的Tris-HCl缓冲体系中,利用热焓放大技术和热动力学初始速率法研究了近生理条件下的乙酰胆碱酯酶(AchE)催化溴化乙酰胆碱水解反应及十二烷基硫酸钠(SDS)对反应的抑制动力学.通过测量实验条件下反应体系的总反应焓及相同条件下的Tris碱的质子化焓,确定了酶反应的摩尔反应焓ΔHm,1为0.63kJ?mol-1,米氏常数Km和底物抑制常数KS分别为0.85~0.94mmol?L-1和0.74~0.83mmol?L-1.SDS能够显著地降低反应速率,但对酶反应的生化常数的影响较小,SDS对AchE的抑制表现为不可逆抑制.在一定浓度的SDS溶液中,AchE的失活符合一级反应动力学规律,表观一级失活速率常数与作用时间及SDS浓度的四次方呈线性关系,失活常数为(2.47~2.69)×1013mol-4?L4?min-1.

 
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