亲和层析柱 meaning in Chinese
affinity column
Examples
- The expressed proteins were purified by ni2 + chelation affinity chromatography . the recombinant proteins were prepared with the purity more than 95 %
用ni ~ nta亲和层析柱进行纯化，获得1 ’ rka膜外域各结构域重组蛋白，纯度均在95 %以上。 - With ni2 + - lda - sepharose , the cbd tag was removed . according to the results of sds - page and western blot analysis , the product of outflow was the target protein lt a 27 . the purity of lt a 27 was about 95 %
运用niz +金属鳌合亲和层析柱进一步快速纯化去除融合头，上样流出经sds一队ge分析和western印迹分析ii1 :明得到的纯化产物为淋巴毒素缺失体蛋白lt凸27 ， lt 2 :产物纯度可达95 %以上。 - But these techniques can not provide physiological ph and ionic strength , and radio - iodination of heparin required for ace endangers health of human and environment . for avoiding the radiological hazards and reflecting directly the binding characteristic of heparin to protein
但亲和层析柱易被污染失活， ace技术不能提供生理ph范围和离子强度及ace技术必需的标记肝素的放射性物质对人和环境具有很大危害。 - After the protein refolding of denaturant inclusion body following dialysis , we got the pure recombinant gst - eo protein by gst affinity columns . using the purified protein as coating antigen , an indirect elisa were developed for detecting the anti - eo antibody in the csfv serum by exploring the concentration of coating an tigen and dilution degree of serum
使用分步透析法对变性的包涵体进行复性，将复性蛋白过gst亲和层析柱得到纯化的gst - eo融合蛋白。以gst - eo融合蛋白为诊断抗原，初步建立了用间接elisa检测猪瘟血清eo抗体的方法。 - The ade + transformants were selected and fermented in flasks with 20ml bmmy medium , then , induced by 0 . 5 % methanol . the expression protein was analyzed by sds - page after five days of induction . sds - page analysis revealed that the high - level expression recombinant strains of pmad16 / pmet a b / abp2304 and pmad16 / pmet a a / abp780 had specific bands at 75kd and 55kd separately , account for 30 % and 10 % of the total protein separately , which were purified using probond resin purification system , and obtained 15mg at levels above 0 . 75g / l and 7mg expression protein at levels above 0 . 35g / l separately once purification , the purity is both above 90 %
筛选ade +表型转化子， 20mlbmmy摇瓶培养，用0 . 5甲醇诱导表达5天后， sds - page检测结果表明：选出的重组高效表达菌株pmad16 pmet b abp2304和pmad16 pmet a abp780都存在明显的表达特异条带，分子量分别为75kd和55kd ，分别占其总蛋白的30和10 ，经过probondresin镍亲和层析柱都得到了纯化，其纯度都在90以上，一次纯化分别可得到大约15mg和7mg表达蛋白，推知表达量分别高达0 . 75g l和0 . 35g l以上。