作业帮英语翻译A cholesterol oxidase (COD) gene from Brevibacterium sp.
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英语翻译
A cholesterol oxidase (COD) gene from Brevibacterium sp.(DQ345780) was expressed in Escherichia coli BL21 (DE3),an affinity protocol was developed for the preparation,and industrial application of this method was of great potential.Riboflavin was chosen as the affinity ligand,and it was coupled with Sepharose 4B through some spacers.With the affinitymedium,the purification process consisted of only one affinity chromatography step to capture the target protein.The purified cholesterol oxidasewas 99.5% pure analyzed on HPLC Vydac C4 column,and 98% with SDS–PAGE analysis.The yield of the expressed enzyme was 9.8% of crude extracted proteins; the recovery of typical cholesterol oxidase activity was 90.1%,higher than that of other reported traditional protocols.Reducing SDS–PAGE analysis showed that the enzyme was a single polypeptide with the mass of ∼50 kDa.The desorption constant Kd and the theoretical maximum absorption Qmax on the affinity medium were 1.0\2g/g medium and 74.5mg/g mediumin absorption analysis.Km and Vmax of cholesterol oxidase activity for the purified enzyme were 25.5\2M and 16.4\2mol/(minmg),respectively.
如果觉得麻烦可以只翻译前面三四句话就好了
A cholesterol oxidase (COD) gene from Brevibacterium sp.(DQ345780) was expressed in Escherichia coli BL21 (DE3),an affinity protocol was developed for the preparation,and industrial application of this method was of great potential.Riboflavin was chosen as the affinity ligand,and it was coupled with Sepharose 4B through some spacers.With the affinitymedium,the purification process consisted of only one affinity chromatography step to capture the target protein.The purified cholesterol oxidasewas 99.5% pure analyzed on HPLC Vydac C4 column,and 98% with SDS–PAGE analysis.The yield of the expressed enzyme was 9.8% of crude extracted proteins; the recovery of typical cholesterol oxidase activity was 90.1%,higher than that of other reported traditional protocols.Reducing SDS–PAGE analysis showed that the enzyme was a single polypeptide with the mass of ∼50 kDa.The desorption constant Kd and the theoretical maximum absorption Qmax on the affinity medium were 1.0\2g/g medium and 74.5mg/g mediumin absorption analysis.Km and Vmax of cholesterol oxidase activity for the purified enzyme were 25.5\2M and 16.4\2mol/(minmg),respectively.
如果觉得麻烦可以只翻译前面三四句话就好了
短杆菌sp.(DQ345780)的胆固醇氧化酶基因在大肠杆菌BL21 (DE3)中进行表达,原位亲和就是为了准备这个实验而开发出来的.该方法的工业应用潜力巨大.选用核黄素作为亲和配体,通过垫片与琼脂糖4b结合.使用该亲和介质后,提纯过程只需亲和层析一个步骤就可完成目标蛋白的提取.提纯后的胆固醇氧化酶用高效液相色谱HPLC Vydac C4 column分析,纯度达到99.5%,用聚丙烯酰胺凝胶（SDS–PAGE ）分析,纯度达到98%.表达的酶量占粗提蛋白质的9.8%；典型胆固醇氧化酶活力恢复程度为90.1%,高于曾经报道过的传统原位技术的数据.简化SDS–PAGE分析表明该酶是一种质量为50kDa的单一多肽.吸收分析中,在亲和介质上解吸常数Kd和理论最大吸收量Qmax分别为1.0\2g/g介质和 74.5mg/g介质.经提纯的胆固醇氧化酶活性Km值和Vmax值分别为 25.5\2M和16.4\2mol/(minmg),
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