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activity recovery     
相关语句
  活力回收
    The activity recovery of the immobilized en- zyme approximatly was 69%.
    固定化酶的活力回收达69%。
短句来源
    Results: PVA served as immobilized carrier of NO. WW-11, and its activity recovery of tryptophanase was 60. 9%.
    结果:以聚乙烯醇作为WW-11的固定化载体,其活力回收为60.9%。
短句来源
    The β-glucanase from strain GXC of Trichoderma reesei was purified in three steps which comprised ammonium sulfate precipitation, Sephadex G-100 chromatography, and DEAE-Sephadex A-50 chromatography. The purified enzyme showed an activity increase of 14.60 fold, and an activity recovery of 6.62%.
    对里氏木霉所产β-葡聚糖酶粗酶液通过饱和硫酸铵沉淀、Sephadex G-100 柱层析和DEAE-Sephadex A-50 柱层析进行纯化,比活提高14.60倍,活力回收6.62%。
短句来源
    The activity of immobilized enzyme was 891 U/g, and enzymatic activity recovery reached 359%. 
    制得的固定化酶活力为89 1U/g载体,酶的活力回收达到35 9%.
短句来源
    β-Galactosidase was immobilized on chitosan microspheres with glutaraldehyde by cross-linking reaction,the immobilezation conditions and characterization of the immobilized enzyme were studide. The optimal conditions for immobilization were as follows:in pH 6.5 P-E-M solution for 10 h,chitosan microsphere was treated with 0.5% glutaraldehde at 25℃ for 12h,the solution of β-Galactosidase was immobilized on the carrier at 4℃ for 12h, enzyme activity recovery was 67%.
    以壳聚糖微球为载体,戊二醛为交联剂,固定β-半乳糖苷酶,对β-半乳糖苷酶的固定化条件及固定化酶的各种性质进行了研究,确定了酶固定的最适条件为:用pH6.5的P-E-M缓冲液浸泡10h,25℃壳聚糖微球与0.5%戊二醛交联12h以上,4℃下酶与壳聚塘微球固定12h以上酶活力回收可达67%。
短句来源
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  活力回收率
    Under optimum conditions for the coupling, the apparent activity and activity recovery of immobllized pectinase were 1980u/g and 87 % respectively.
    在以上最适条件下,固定化果胶酶的表观活力为1980U/g,活力回收率为87%。
短句来源
    When the amount of lipase is between 168u/g silk to 308u/g silk,the activity of immobilized lipase is between 106u/g silk to 160u/g silk and the activity recovery is quite high (above 52%).
    加酶量为168~308u/g蚕丝时,所得固定化脂肪酶活力为106~160u/g蚕丝,此时固定化酶的活力回收率较高(>52%)。
短句来源
    The optimum conditions for immobilization were as follows: Chitosan was treated with 5% solution of qlutaraldehyde at 30℃ for 8h, then 10ml solution of trypsin (0.3mg/ml pH7. 0 ) was inunobilized on the carrier. Enzyme activity recovery was 67 %~75%.
    5%戊二醛在30℃下处理载体8h,加10ml酶液(0.3mg/ml,pH7.0)固定12h以上,活力回收率达67%-75%。
短句来源
    The results were as follows: the optimum load of enzyme was 1.92 mg enzyme/g carrier, the absorbing time was 12 h and the temperature 4~8 ℃; then interacted for 3 h at 4~8 ℃ with 0.5% glutaraldehyde. The activity and the activity recovery of the immobilized papain were 38.49 U/g carrier and 66.60% respectively.
    结果显示 :木瓜蛋白酶的最佳固定化条件是给酶量为 1 .92mg/g、4~ 8℃吸附 1 2h、再用体积分数为 0 .5 %的戊二醛溶液于 4~ 8℃交联 3h ,所制得的固定化木瓜蛋白酶活力达 38.49U/g ,酶活力回收率平均达 6 6 .6 0 % ,高于同类研究水平
短句来源
    In order to investigate the recognition mechanism and the relationship between structure and function of tRNA Trp with tryptophanyl tRNA synthetase (TrpRS), TrpRS from Bacillus subtilis was purified and immobilized on CNBr activated Sepharose 4B. Protein recovery and activity recovery of the immobilization were 95.5% and 31.3%, respectively. Properties of immobilized TrpRS were studied in detail.
    为研究tRNATrp 与色氨酰tRNA合成酶(TrpRS) 的相互识别及其结构、功能关系, 纯化了枯草杆菌TrpRS并用溴化氰活化的Sepharose 4B 将TrpRS固定化, 固定化TrpRS的蛋白质回收率为95 .5 % , 活力回收率为31.3% 。
短句来源
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  活性回收率
    The results showed the optimum immobilized α-Acetolactate decarboxylase being 20 mL/g the magnetic microspheres,0.98 % glutaraldehyde,in which the activity of immobilized α-Acetolactate decarboxylase was 65 180 U/g,the specific activity was 872.32 U/mg and the activity recovery was 42.33%.
    结果显示,在酶固定化过程中,自由酶的添加量为20 mL/g微球,戊二醛的添加量为0.98%。 在其固定化最佳条件下,制备的固定化ALDC的活力为65 180 U/g,而且其比活、活性回收率分别可达872.32 U/mg和42.33%。
短句来源
    The protein mass yield of rhIFNα-2b under the optimum condition was 4.2 times higher than that of dialysis refolding process. The activity recovery rate was 68.7% with the specific activity of 1.77×108IU/mg,and purity of 90%.
    结果表明,复性后rhIFNα-2b的蛋白收率是透析复性法的4.2倍,活性回收率为68.7%,比活力1.77×108IU/mg,纯度高于90%。
短句来源
    It was shown that the specific activity of immobilized trypsin on chitosan was 3 936.4 6BAEE/mg,and the activity recovery of trypsin was 70.81%. The activity rate of aprotinin is 114.37 times higher than that of the tissue extrac.
    抑肽酶抑制比活单位(BAEE/mg)为3 936.46,酶活性回收率70.81%,最后的纯化倍数达到114.37倍。
短句来源
    RESULTS 2 49 mg final product was homogeneous by the criterion of SDS PAGE representing the 12.46% yield and 13.68% activity recovery from 1000 mL serum.
    结果 成功地从 1L血浆中提纯到了 2 .49m g C2 ,产率为 12 .46 % ,活性回收率为 13.6 8% .
短句来源
    The purity ,specific activity,recovery rate of activity,relative molecular weight (M.W)and PI were over 98%,2.4×10 7IU/mg, 14%,19800 and 5.0 respectively .
    纯化的rhIFN α1b的纯度为 98%以上 ,比活性 2 .4× 10 7IU/mg ,活性回收率 14 % ,相对分子质量 1980 0和等电点 5 .0。
短句来源
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  活力恢复
    the highest recovery of activity was at a molar ratio of A and B chains of 1.5:1. The final reoxidation product thus obtained usually had an activity of 12 international units/mg of total protein, about 50% of that of crystalline insulin. The optimal reduction and reoxidation conditions for activity recovery established so far were: 1) reduction with 28-fold excess of mercaptoethanol at 100℃, pH 5 for 6min.
    将经过分离提纯的A及B链按不同比例重新混合还原重氧化结果表明活力恢复程度与A与B链的比例有关,A比B过量对活力恢复有利,A:B=1.5:1时活力恢复最高,可达天然胰岛素的50%左右。
短句来源
    Results show that the activity recovery of (Na++ K+ ) - ATPase is maximum, medium and minimum when reconstituted with soybean phosph-olipids, acidic phospholipid of PG and neutral phospholipid of DPPC respectively.
    结果表明. 用大豆磷脂重组的(Na~++K~+)-ATP酶活力恢复最大;
短句来源
    Under suitable conditions, an activity recovery of 90% can be obtained.
    在适当条件下,酶的活力恢复可达90%以上。
短句来源
    A comparison of the rate constants for the refolding of the molecule with those for the recovery of its enzymatic activity shows that they are not synchronized and the activity recovery approaches completion after the refolding and dimerization of the subunits as detected by the methods employed.
    将用荧光、CD和紫外差吸收监测的构象变化与活力变化的速度常数比较,表明酶活力恢复前期的速度与构象变化速度相当,但在酶分子的总体构象变化完成之后,活力恢复尚未完全。
短句来源

 

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      activity recovery
    Addition of the same concentration of polysorbate 80 to the reconstitution medium caused an increase in activity recovery for each formulation, but the overall pattern remained unchanged.
          
    Annealing of sucrose-glycine formulations causes a small but significant decrease in activity recovery relative to unannealed controls, whereas no annealing effect is observed with sucrose-only formulations.
          
    In a sucrose-only excipient system, activity recovery of both model proteins is about 80% and is independent of sucrose concentration over a range from 1 to 40 mg/mL.
          
    However, the high activity recovery in the presence of detergents, as the stripping agent, suggests that they can constitute suitable replacement for the more expensive and common stripping agent of cyclodextrins.
          
    These findings may assist the activity recovery of recombinant proteins at relatively high concentrations.
          
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    The S-sulphonates of A and B chains obtained by splitting insulin with Na_2SO_3 and Na_2S_4O_6 in the absence of urea were separated by repeated precipitation of the B chain at pH 6.4. From the supernatant solution, the A chain was further purified by zone electrophoresis on cellulose powder at pH 7. When the S-sulphonates of A and B chains were mixed, reduced and reoxidized the final level of activity regenerated varied with the ratio of the chains; the highest recovery of activity was at a molar ratio of A...

    The S-sulphonates of A and B chains obtained by splitting insulin with Na_2SO_3 and Na_2S_4O_6 in the absence of urea were separated by repeated precipitation of the B chain at pH 6.4. From the supernatant solution, the A chain was further purified by zone electrophoresis on cellulose powder at pH 7. When the S-sulphonates of A and B chains were mixed, reduced and reoxidized the final level of activity regenerated varied with the ratio of the chains; the highest recovery of activity was at a molar ratio of A and B chains of 1.5:1. The final reoxidation product thus obtained usually had an activity of 12 international units/mg of total protein, about 50% of that of crystalline insulin.The optimal reduction and reoxidation conditions for activity recovery established so far were: 1) reduction with 28-fold excess of mercaptoethanol at 100℃, pH 5 for 6min. 2) precipitation and washing of the reduced chains at pH 3.8.3) reoxidation at 3-5℃ in pH 10.6 glycine buffer at a protein concentration of 5mg/ml.The velocities of the reduction and reoxidation of respectively the S-sulphonated and reduced B chain alone were consider(?)bly slower than those of the corresponding A chain derivatives alone but were raised to the level of those of the A chain derivatives in mixtures of the chains. These and the regeneration of about 50% of insulin activity from the reduced chains under favourable conditions suggest strongly that some interactions between the chains, probably through secondary bonds, take place in solution. These interactions may play an important role in the successful resynthesis of insulin from its chains.

    利用二者溶解度的不同可以将无脲条件下拆开的胰岛素初分而得到较纯的S-磺酸型A及B链,再在中性pH用纤维素板电泳可以制得纯的S-磺酸型A链。将经过分离提纯的A及B链按不同比例重新混合还原重氧化结果表明活力恢复程度与A与B链的比例有关,A比B过量对活力恢复有利,A:B=1.5:1时活力恢复最高,可达天然胰岛素的50%左右。本文还对从S-磺酸型A及B链重合成胰岛素最有利的还原及重氧化条件进行了探讨,除其他条件外重氧化的最适pH为10.6。B链单独存在时其还原及重氧化速度均明显地较A链的相应速度为低,但二者共同存在时的还原及重氧化速度却与A链单独存在时相同,表明在溶液中自由A及B链间存在着对恢复活力有重要影响的相互作用,可能是通过次级链作用的相互作用。

    Polynucleotide phosphorylase(PNPase)from E.Celi 1.183 was coupled to diazo-tized p-aminobenzenesulphonylethyl(ABSE)agarose.Its activity recovery and stabi-lity were superior to those of PNPase immobilized on ABSE-Sephadex G-200 andABSE-cellulose.Upon immobilization,the optimum pH for the polymerization shifted from 9.6to 10.The free enzyme showed maximum activity at 47℃,whereas the optimumtemperature of the immobilized enzyme became rather broad,between 42~52℃.Theapparent K_m of the immobilized enzyme...

    Polynucleotide phosphorylase(PNPase)from E.Celi 1.183 was coupled to diazo-tized p-aminobenzenesulphonylethyl(ABSE)agarose.Its activity recovery and stabi-lity were superior to those of PNPase immobilized on ABSE-Sephadex G-200 andABSE-cellulose.Upon immobilization,the optimum pH for the polymerization shifted from 9.6to 10.The free enzyme showed maximum activity at 47℃,whereas the optimumtemperature of the immobilized enzyme became rather broad,between 42~52℃.Theapparent K_m of the immobilized enzyme was same as the free enzyme.The immobilizedenzyme appeared to be more heat stable than the free enzyme.After treatment at 57℃for 30 min,the retained activity of the immobilized enzyme was 72% while that ofthe free enzyme was 22%.

    对-重氮基苯磺酰乙基琼脂糖是制备固定化多核苷酸磷酸化酶的较好材料,与具有同样活性基团的纤维素和葡聚糖凝胶G200相比,活力回收高、稳定性好。固定化酶的最适pH 向偏碱的方向转移,最适温度较自然酶为宽,表观米氏常数与自然酶基本一致。57℃保温30分钟尚保留70%以上的活力,而自然酶仅剩余22%的活力,说明稳定性有所提高。

    1. p-aminobenzene sulphonyl ethyl-(ECD)-agar has been obtained by reaction of 8% epichrolohydrin-orosslinked desulphate (ECD) agar with p, β-(sulphato ethyl sulohonyl) aniline (SESA) in an alkaline medium at above 60%. The optimal pH of etherization is 10. A series of ABSE-(ECD)-agar possessing 107-1216 μmoles of aromatie amine/g dry weight of support have been prepared by controlling the amount of SESA added.2. The diazonium salts of ABSE-(ECD)-agar easily coupled with nuclease P_1 at pH 6.4-8.0. The activity...

    1. p-aminobenzene sulphonyl ethyl-(ECD)-agar has been obtained by reaction of 8% epichrolohydrin-orosslinked desulphate (ECD) agar with p, β-(sulphato ethyl sulohonyl) aniline (SESA) in an alkaline medium at above 60%. The optimal pH of etherization is 10. A series of ABSE-(ECD)-agar possessing 107-1216 μmoles of aromatie amine/g dry weight of support have been prepared by controlling the amount of SESA added.2. The diazonium salts of ABSE-(ECD)-agar easily coupled with nuclease P_1 at pH 6.4-8.0. The activity recoveries of immobilized nuclease P_1 were 18-35%. In this case, 1 g of support can bind 105-120mg of protein and 4280 units of nuclease P_1.3. In the coupling reaction, the presence of ammonium in the medium could increase the activity of immobilized nuclease P_1, but its stability was less than that of the control.4. The support containing 1216 μmoles aromatic amine per gram of agar bound more protein, but the immobilized enzyme showed less biological activity.5. α-naphthol was used to "block" the residual diazonium salts on the immobilized enzymes. The stability of immobilized nuclease P_1 thus obtained was distinctly improved.

    1.8%琼脂经环氧氯丙烷交联后,在碱性条件下与对β-硫酸酯乙砜基苯胺(SESA)反应制得了对氨基苯磺酰乙基-(ABSE)-交联琼脂。醚化反应最适pH是10。控制SESA加入量制得含有107~1216微克分子苯胺基/克干重琼脂载体。2.ABSE-交联琼脂经重氮化后可在pH6.4~8.0偶联核酸酶P_1,每克琼脂可结合105~120毫克核酸酶P_1,固定化酶活力为4280单位/克干重固定化酶。活力回收可达18~35%。3.偶联时硫酸铵的存在可稍微提高固定化核酸酶P_1的活力,但其稳定性却比对照的差。4.载体上苯胺基含量过多会不利于所固定化的酶显示活力,用α-萘酚封闭残留的苯胺基,可以明显增加固定化酶的稳定性。

     
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