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For determination of optimal L-cysteine sulfinic acid concentration in the staining mixture, samples of AAT extracted from pea cv. Bohat~rr were chosen, which showed the most disadvantageous ratio of AAT activity to protein content (Table 1.) The critical amount of this sample for loading to 15-well-comb for electrophoresis was found to be 4 - 5 gl (approximately 40 Ixg of protein) without considerable streaking of the isozyme bands. Fig. 1 shows the influence of L-cysteine sulfinic acid concentration and staining time on intensity of isozyme bands. The possible increasing of developing time with decreasing CSA concentration is evident. In the ease of 0.05 M CSA the staining time is limited to 30 min, after which the staining mixture precipitated together with increasing background staining. Two slow migrating zones of AAT activity are comparably fainter in 0.05 M CSA than in 0.025, 0.01 and 0.005 M CSA, whichcould be explained as inhibition by the substrate or by the product, respectively, of enzymatic reaction of these two active isozymes, in contrast to the fast migrating fine triplet, which is equally stained in all concentrations of CSA mentioned above. In the case of 0.0025 M CSA all isozyme bands are fainter than in higher concenlrations of CSA, which suggests insufficient amount of the substrate for enzyme reaction and following electron transfer to form insoluble formazan. The reaction mixturecontaining 0.05 M CSA precipitated and inactivated at 20 - 30 rain in contrast to lower CSA concentrations (40 - 150 rain). This could be caused either by CSA itseff or by overproduction of the reducing agent (I-ISO3") which can lead to non-specific reduction of MTT in the solution. The blank experiments were not carried out as this was not a subject of the study. Using 0.025, 0.01 and 0.005 M L-cysteine snlfinic acid in the reaction mixture, together with prolonging the developing lime, we can obtain practically the same results in intensity and sensitivity of isozyme staining. 0.01 M CSA seems to be a good compromise between the cost of the substrate used and staining time, but 0.005 M CSA also gave acceptable results. 0.025 M CSA is a relatively rapid and sensitive variant without danger of fast backgroundoverstaining. We also tested detection limits for the two procedures (Fig. 2) using serial dilutions of soybean seed sample. We noted a gradual decrease in intensity of isozyme staining over the whole dilution range (0 - 32 x) with CSA staining, whilenotable bands with classical staining were recorded only till the dilution 8 x. As comparable result for dilution 32 x (CSA) we can consider 4 - 8 x (Fast Blue BB). This shows that staining using L-eysteine sulfinic acid is approximately 4 - 8 fold more sensitive than the standard one in this arrangement of the experiments.
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Answer 1

测定l -半胱氨酸的最佳sulfinic酸浓度在染色混合物,样品提取豌豆AAT简历。Bohat ~ rr选择显示,最不利的比率,蛋白质含量AAT活动(表1)。临界量的这个示例加载到15-well-comb对电泳被发现是4 - 5 gl(约40 Ixg的蛋白质),没有相当的裸奔的同工酶乐队。图1显示了l -半胱氨酸的影响sulfinic酸浓度、染色时间在强度的同工酶乐队。开发时间的增加可能与减少CSA浓度是显而易见的。易用性0.05 CSA泪痕的时间是有限的,30分钟后,染色混合在一起沉淀与增加背景染色。两个缓慢的活动迁移区AAT也相当微弱0.05 CSA比0.025,0.01和0.005 M CSA,其中可能被解释为基质的抑制或产品,分别酶促反应的这两个活跃的同工酶,相对于快速迁移好三连音,这也是所有的染色浓度CSA上面提到的。在案件的0.0025 M CSA所有同工酶带在高等concenlrations比它暗的修正案,这表明数量的不足的基质,电子转移酶反应后形成不溶性formazan。0.05 mixturecontaining反应CSA沉淀和灭活在20 - 30雨与浓度较低的CSA(40 - 150下雨)。 这可能导致通过CSA itseff或生产过剩的还原剂(I-ISO3”)会导致非特异性减少MTT在解决方案。空白实验没有调整,这不是一个研究的主体。使用0.025、0.01和0.005 M l -半胱氨酸snlfinic酸反应混合物,连同延长发展中石灰,我们可以获得几乎相同的结果在强度和同工酶的敏感性

Answer 2

测定l -半胱氨酸的最佳sulfinic酸浓度在染色混合物,样品提取豌豆AAT简历。Bohat ~ rr选择显示,最不利的比率,蛋白质含量AAT活动(表1)。临界量的这个示例加载到15-well-comb对电泳被发现是4 - 5 gl(约40 Ixg的蛋白质),没有相当的裸奔的同工酶乐队。图1显示了l -半胱氨酸的影响sulfinic酸浓度、染色时间在强度的同工酶乐队。开发时间的增加可能与减少CSA浓度是显而易见的。易用性0.05 CSA泪痕的时间是有限的,30分钟后,染色混合在一起沉淀与增加背景染色。两个缓慢的活动迁移区AAT也相当微弱0.05 CSA比0.025,0.01和0.005 M CSA,其中可能被解释为基质的抑制或产品,分别酶促反应的这两个活跃的同工酶,相对于快速迁移好三连音,这也是所有的染色浓度CSA上面提到的。在案件的0.0025 M CSA所有同工酶带在高等concenlrations比它暗的修正案,这表明数量的不足的基质,电子转移酶反应后形成不溶性formazan。0.05 mixturecontaining反应CSA沉淀和灭活在20 - 30雨与浓度较低的CSA(40 - 150下雨)。这可能导致通过CSA itseff或生产过剩的还原剂(I-ISO3”)会导致非特异性减少MTT在解决方案。空白实验没有调整,这不是一个研究的主体。使用0.025、0.01和0.005 M l -半胱氨酸snlfinic酸反应混合物,连同延长发展中石灰,我们可以获得几乎相同的结果在强度和灵敏度的同工酶染色。0.01 CSA似乎是一个很好的折衷成本之间的基质、染色时间使用,但0.005 CSA也给了可接受的结果。0.025 CSA是一个相对快速、敏感的快速backgroundoverstaining变体没有危险。我们还测试了检测极限的两个程序(图2)使用串行稀释大豆种子样本。我们注意到在强度逐渐下降趋势的同工酶染色在整个稀释范围(0 - 32 x)和CSA染色,染色whilenotable乐队与古典的记录只直到稀释8倍。堪比结果稀释32 x(CSA)我们可以考虑4 - 8 x(快速蓝色BB)。这表明,使用L-eysteine染色sulfinic酸是大约4 - 8折比标准更敏感的实验在这种安排。