Fig. 1B Figure 1B (a and b) shows t

Fig. 1B Figure 1B (a and b) shows the results using 2 M urea/PBS pH 7.4. Under these solvent conditions, 26.8 ±% and 25.9 ±% of I-AC and I-PC respectively bound to the column in the native state (Table 1). The results indicate that 26% – 27% of collagen molecules could bindound to TiO2, irrespective of telopeptide. But after heat denaturation, these bound ratio amounts of I-AC and I-PC decreased to 17.2 ± 3.2 % and 11.6 ±2.5 %, respectively (Add the statistical analysis). Add the statistical analysis! Fig. 1C Figure 1C (a and b) shows the results with 2 M urea/HCl, pH 3.0. Even with this more potent dissociative solvent, 27.1 ±3.5 %, and 17.0 ±2.3 %, of the native I-AC and denatured I-AC, respectively, bound to the column (Table 1). This difference indicates that considerable amounts (17 – 27%) of I-AC molecules could link with TiO2, in this more robust dissociative condition. With I-PC, the percentages of bound collagen were markedly higher at 40.8 ±3.5 % and 24.1±2.3 % for native and denatured forms, respectively. We noticed that wWith all the native collagens, some tailing-peaks accompanied the pass-through peaks but with the denatured collagens, these were not observed (Figs. 1A – 1C). Table 1 Table 1 summarizes the percentages of the various collagens bound to Ti-binding percent of the various collagens with the three different solvents, totaling six categories: acid-soluble collagen (AC), pepsin solubilized collagen (PC), both of which include native and denatured collagens, each of which we chared on the column with three different solvents: dilute HCl, 2 M urea/PBS and 2M urea/HCl (pH 3.0). The figures indicate the ratio s (%) of the chromatographic area of the bound fraction (wash-out peaks with 0.025 M NaOH) to the total areas of the applied sample (sum of pass-through fractions and bound fraction), which corresponds to the strength of the Ti-binding the ability of each collagen. Comment 4-2 【P13, L13~P15, L2】-2【Dis to Res】There seemed appeared to be no essential difference in the results of chromatographic profiles with betweenof the three different solvents used as eluents. However, we found remarkable differences between the ratios of the pass-through fraction and wash-out peaks (the binding ratios) before and after heat denaturation. In the case of the native pepsin solubilized collagen (I-PC), we noticed observed that the binding ratio showed the highest value of 40.8 ±3.5% adsorption in 2 M urea (pH 3.0), while the Ti-binding ratio reduced to 24.1±2.3 % after heat denaturation. 【Dis to Res】 Comment 2/4-23 【P13, L13~P15, L2】-3 【Dis to Res】 Most interestingly, the Ti-binding ratios decreased after denaturation. These changes occurred in with all collagens analyzed, under with all three solvents, regardless of the presence of telopeptides. , Aas summarized in Table 1,. T and Fig. 2, we have shown for the first timethis is the first evidence that type I collagen can bind with to TiO2 in diluted HCl (pH. 4.0), 2 M urea (pH 7.4) and 2 M urea /HCl (pH 3.0). It is apparent that , tMoreover, the and that the Ti-binding ratio diminished to approximately 2/3 after the denaturation of the collagen and . Wwe obtained the same tendency ofa similar reduction of the Ti-binding ratio after denaturation in I-AC and I-PC. , as shown in Figure 2 and Table 1. showed shows that binding ratios 30.4, 26.8 and 27.1% of native collagens (I-AC), in pH 4.0 (HCl), pH 7.4 (2 M urea), and pH 3.0 (2 M urea) before denaturation. These Ti-binding ratios reduced after denaturation, to 19.3, 17.3 and 17.0%, in pH 4.0 (HCl), pH 7.4 (2 M urea) and pH 3.0 (2 M urea), respectively. These reductions were all statistically significant with Student's test, with p values of 0.003, 0.0015, and 0.028, with respect to the three different solvents..Comment 4-2【P13, L13~P15, L2】-4【Dis to Res】 We observed a reduction of the Ti-binding ability with I-PC. The results showed that before denaturation, 32.2, 25.9%, and 40.8% of I-PC were bound to the Ti column, in pH. 4.0 (HCl), pH 7.4 (2 M urea) and pH 3.0 (2 M urea), respectively. But, after denaturation, these binding ratios were reduced to 20.6, 11.6, and 24.1% in the above solvents, respectively (Fig. 2 and Table 1). 【Above three paragraphs (2/4-2, 2/4-3, and 2/4-4) were moved from Dis to Res (at the end of chromate-session)】DO NOT REPEAT ADDSTATI Comment 52-4/4 【p16, L14~P17, L3】-4【Dis to Res】As for tThe importance of requirement for functional of telopeptides in the binding, we obtained clear informationis indicated by comparing comparison of the chromatograms of I-AC and PC in the different solvents.. When we used dilute HCl (pH 4.0) was used as a solvent, the Ti-binding ratios between I-AC (30.4%) and PC (32.2%) were not significantly different (p: 0.56). This difference was much smaller in the denatured collagen, being 19.3% in I-AC and 20.6% in I-PC (p: 0.72). However, in the dissociative solvent of 2 M urea / HCl (pH 3.0), the percentag

Fig. 1B Figure 1B (a and b) shows the results using 2 M urea/PBS pH 7.4. Under these solvent conditions, 26.8 ±% and 25.9 ±% of I-AC and I-PC respectively bound to the column in the native state (Table 1). The results indicate that 26% – 27% of collagen molecules could bindound to TiO2, irrespective of telopeptide. But after heat denaturation, these bound ratio amounts of I-AC and I-PC decreased to 17.2 ± 3.2 % and 11.6 ±2.5 %, respectively (Add the statistical analysis). Add the statistical analysis! Fig. 1C Figure 1C (a and b) shows the results with 2 M urea/HCl, pH 3.0. Even with this more potent dissociative solvent, 27.1 ±3.5 %, and 17.0 ±2.3 %, of the native I-AC and denatured I-AC, respectively, bound to the column (Table 1). This difference indicates that considerable amounts (17 – 27%) of I-AC molecules could link with TiO2,  in this more robust dissociative condition. With I-PC, the percentages of bound collagen were markedly higher at 40.8 ±3.5 % and 24.1±2.3 % for native and denatured forms, respectively. We noticed that wWith all the native collagens, some tailing-peaks accompanied the pass-through peaks but with the denatured collagens, these were not observed (Figs. 1A – 1C). Table 1  Table 1 summarizes the percentages of the various collagens bound to Ti-binding percent of the various collagens with the three different solvents, totaling six categories: acid-soluble collagen (AC), pepsin solubilized collagen (PC), both of which include native and denatured collagens, each of which we chared on the column with three different solvents: dilute HCl, 2 M urea/PBS and 2M urea/HCl (pH 3.0). The figures indicate the ratio s (%) of the chromatographic area of the bound fraction (wash-out peaks with 0.025 M NaOH) to the total areas of the applied sample (sum of pass-through fractions and bound fraction), which corresponds to the strength of the Ti-binding the ability of each collagen. Comment 4-2 【P13, L13~P15, L2】-2【Dis to Res】There seemed appeared to be no essential difference in the results of chromatographic profiles with betweenof the three different solvents used as eluents. However, we found remarkable differences between the ratios of the pass-through fraction and wash-out peaks (the binding ratios) before and after heat denaturation. In the case of the native pepsin solubilized collagen (I-PC), we noticed observed that the binding ratio showed the highest value of 40.8 ±3.5% adsorption in 2 M urea (pH 3.0), while the Ti-binding ratio reduced to 24.1±2.3 % after heat denaturation. 【Dis to Res】 Comment 2/4-23 【P13, L13~P15, L2】-3 【Dis to Res】 Most interestingly, the Ti-binding ratios decreased after denaturation. These changes occurred in with all collagens analyzed, under with all three solvents, regardless of the presence of telopeptides. , Aas summarized in Table 1,. T and Fig. 2, we have shown for the first timethis is the first evidence that type I collagen can bind with to TiO2 in diluted HCl (pH. 4.0), 2 M urea (pH 7.4) and 2 M urea /HCl (pH 3.0). It is apparent that , tMoreover, the and that the Ti-binding ratio diminished to approximately 2/3 after the denaturation of the collagen and . Wwe obtained the same tendency ofa similar reduction of the Ti-binding ratio after denaturation in I-AC and I-PC. , as shown in Figure 2 and Table 1. showed shows that binding ratios 30.4, 26.8 and 27.1% of native collagens (I-AC), in pH 4.0 (HCl), pH 7.4 (2 M urea), and pH 3.0 (2 M urea) before denaturation. These Ti-binding ratios reduced after denaturation, to 19.3, 17.3 and 17.0%, in pH 4.0 (HCl), pH 7.4 (2 M urea) and pH 3.0 (2 M urea), respectively. These reductions were all statistically significant with Student's test, with p values of 0.003, 0.0015, and 0.028, with respect to the three different solvents..Comment 4-2【P13, L13~P15, L2】-4【Dis to Res】 We observed a reduction of the Ti-binding ability with I-PC. The results showed that before denaturation, 32.2, 25.9%, and 40.8% of I-PC were bound to the Ti column, in pH. 4.0 (HCl), pH 7.4 (2 M urea) and pH 3.0 (2 M urea), respectively. But, after denaturation, these binding ratios were reduced to 20.6, 11.6, and 24.1% in the above solvents, respectively (Fig. 2 and Table 1). 【Above three paragraphs (2/4-2, 2/4-3, and 2/4-4) were moved from Dis to Res (at the end of chromate-session)】DO NOT REPEAT ADDSTATI Comment 52-4/4  【p16, L14~P17, L3】-4【Dis to Res】As for tThe importance of requirement for functional of telopeptides in the binding, we obtained clear informationis indicated by comparing comparison of the chromatograms of I-AC and PC in the different solvents.. When we used dilute HCl (pH 4.0) was used as a solvent, the Ti-binding ratios between I-AC (30.4%) and PC (32.2%) were not significantly different (p: 0.56). This difference was much smaller in the denatured collagen, being 19.3% in I-AC and 20.6% in I-PC (p: 0.72). However, in the dissociative solvent of 2 M urea / HCl (pH 3.0), the percentag

0/5000

源语言: -

目标语言: -

结果 (简体中文) 1: [复制]

复制成功！

图1B 图1B（a和b）显示了使用2 M尿素/ PBS pH 7.4的结果。在这些溶剂条件下，26.8±％和25.9±％的I-AC和I-PC分别以天然状态结合到色谱柱上（表1）。结果表明，与端肽无关，26％– 27％的胶原分子可以与TiO2结合。但是在热变性后，这些I-AC和I-PC的结合比率分别降低到17.2±3.2％和11.6±2.5％（添加统计分析）。添加统计分析！ 图1C 图1C（a和b）显示了使用2 M尿素/ HCl（pH 3.0）的结果。即使使用这种更有效的解离溶剂，天然I-AC和变性I-AC仍分别与色谱柱结合（表1），分别为27.1±3.5％和17.0±2.3％。这种差异表明，在这种更稳定的解离条件下，大量的I-AC分子可以与TiO2连接。使用I-PC，天然和变性形式的结合胶原蛋白的百分比分别显着更高，分别为40.8±3.5％和24.1±2.3％。 我们注意到，在所有天然胶原蛋白的作用下，一些峰尾都伴随有通过峰，而对于变性胶原蛋白，则未观察到这些峰（图1A – 1C）。 表格1 表1总结了用三种不同溶剂与各种胶原蛋白的钛结合百分比结合的各种胶原蛋白的百分比，共计六类：酸溶性胶原蛋白（AC），胃蛋白酶增溶的胶原蛋白（PC），两者均包括天然胶原蛋白变性的胶原蛋白，我们将每种胶原蛋白用三种不同的溶剂在色谱柱上炭化：稀盐酸，2 M尿素/ PBS和2M尿素/ HCl（pH 3.0）。该图表示结合的馏分（0.025 M NaOH的洗脱峰）的色谱面积与所施加样品总面积（通过馏分和结合馏分的总和）之比s（％）。 Ti的强度结合每种胶原蛋白的能力。 注释4-2【P13，L13〜P15，L2】-2【Dis to Res】 用三种不同的溶剂作为洗脱液，色谱图谱的结果似乎没有本质上的区别。但是，我们发现热变性前后的通过率与洗脱峰之比（结合率）之间存在显着差异。在天然胃蛋白酶溶解的胶原蛋白（I-PC）的情况下，我们注意到观察到结合率在2 M尿素（pH 3.0）中显示出最高的40.8±3.5％吸附值，而Ti的结合率降至24.1热变性后为±2.3％。 【Dis to Res】评论2 / 4-23【P13，L13〜P15，L2】-3【Dis to Res】 最有趣的是，变性后Ti的结合率降低。这些变化发生在所有三种溶剂下分析的所有胶原蛋白中，无论端肽是否存在。，Aas总结在表1中。T和图2，我们首次展示了这是I型胶原可以在稀释的HCl（pH。4.0），2 M尿素（pH 7.4）和2 M尿素/ HCl（pH 3.0）。显然，此外，在胶原和胶原变性后，Ti和Ti的结合率降低到约2/3。在I-AC和I-PC变性后，我们获得了类似的Ti结合率降低的趋势。，如图2和表1所示，表明在pH 4.0（HCl），pH 7.4（2 M尿素）和pH 3中，天然胶原蛋白（I-AC）的结合率分别为30.4、26.8和27.1％。变性前为0（2 M尿素）。变性后，在pH 4.0（HCl），pH 7.4（2 M尿素）和pH 3.0（2 M尿素）中，这些Ti结合率分别降低至19.3％，17.3和17.0％。这些减少量在学生检验中均具有统计学意义，相对于三种不同的溶剂，p值分别为0.003、0.0015和0.028。 注释4-2【P13，L13〜P15，L2】-4【从Dis到Res】 我们观察到I-PC的Ti结合能力降低。结果表明，在变性之前，pH值为32.2、25.9％和40.8％的I-PC与Ti柱结合。分别为4.0（HCl），pH 7.4（2 M尿素）和pH 3.0（2 M尿素）。但是，变性后，在上述溶剂中，这些结合率分别降低到20.6、11.6和24.1％（图2和表1）。【以上三段（2 / 4-2、2 / 4-3和2 / 4-4）从Dis移至Res（在铬酸盐处理结束时））不要重复添加 STATI评论52-4 / 4【p16，L14〜P17，L3】-4【显示为分辨率】 至于结合中对端肽功能的要求的重要性，通过比较不同溶剂中I-AC和PC的色谱图，我们获得了清晰的信息。当我们使用稀HCl（pH 4.0）作为溶剂时，在溶剂中，I-AC（30.4％）和PC（32.2％）之间的Ti结合率没有显着差异（p：0.56）。变性胶原蛋白的差异小得多，在I-AC中为19.3％，在I-PC中为20.6％（p：0.72）。但是，在2 M尿素/ HCl（pH 3.0）的解离溶剂中，

正在翻译中..

结果 (简体中文) 2:[复制]

复制成功！

图 1B 图 1B（a 和 b）显示使用 2 M 尿素/PBS pH 7.4 的结果。在这些溶剂条件下，26.8 ±% 和 25.9 ±% 的 I-AC 和 I-PC 分别绑定到本机状态的柱（表 1）。结果表明，26%~27%的胶原蛋白分子可以与TiO2结合，而与特洛普肽无关。但热变性后，I-AC和I-PC的这些约束比量分别降至17.2±3.2%和11.6±2.5%（加上统计分析）。添加统计分析！ 图 1C 图 1C（a 和 b）显示了 200 万尿素/HCl、pH 3.0 的结果。即使使用这种更强的分离溶剂，27.1±3.5% 和 17.0 ±2.3% 的原生 I-AC 和变性 I-AC 分别绑定到列（表 1）。此差异表示数量相当多（17 ~ 27%）I-AC分子可以与TiO2连接，在这个更健壮的分离条件下。在I-PC中，绑定胶原蛋白的比例明显高于40.8±3.5%和24.1±2.3%的原生形式和变性形式。 我们注意到，与所有的原生胶原蛋白，一些尾峰伴随着通过峰，但与变性胶原蛋白，这些没有观察到（图1A+1C）。 表1 表1总结了与三种不同溶剂结合各种胶原蛋白的Ti结合百分比的各种胶原蛋白的百分比，共六类：酸溶胶原蛋白（AC）、肽溶胶原蛋白（PC），两类均包括原生胶原蛋白和变性胶原蛋白，每种用三种不同的溶剂在柱子上烧焦：稀释HCl、2M尿素/PBS和2M尿素/HCl（pH 3.0）。这些数字表明比率为 s （%）结合分数的色谱面积（用 0.025 M NaOH 洗出峰值）到应用样本的总面积（直通分数和绑定分数的总和），对应于 Ti 结合每个胶原蛋白的能力强度。 注释 4-2 [P13， L13]P15， L2{-2}[Dis 到 Res] 色谱剖面的结果似乎与用作洗水剂的三种不同溶剂之间没有本质的区别。然而，我们发现在热变性之前和之后，直通分数和洗涤峰（结合比）的比率之间存在显著差异。在原生辣椒溶解胶原蛋白（I-PC）的情况下，我们注意到，结合比在2M尿素（pH 3.0）中表现出最高值40.8±3.5%吸附率，而Ti结合比在热变性后降低到24.1±2.3%。 [拒绝 Res] 注释 2/4-23 [P13， L13]P15， L2=-3 [拒绝到 Res] 最有趣的是，变性后，Ti 结合比率下降。这些变化发生在所有胶原蛋白分析下，所有三种溶剂下，无论存在特洛普肽。，Aas 在表 1 中总结。T 和图 2，我们首次表明，这是第一个证据， I 型胶原蛋白可以结合与 TiO2 在稀释的 HCl （pH. 4.0）， 2 M ure

正在翻译中..

结果 (简体中文) 3:[复制]

复制成功！

图1B 是的 图τ1B®（a和b）显示了使用2 M尿素/PBS pH 7.4的结果。在这些溶剂条件下，I-AC和I-PC在天然状态下分别为26.8±%和±25.9±结合在柱上（表1）。结果表明，26%-27%的胶原分子可与TiO2结合，与telopeptide®无关，但热变性后，I-AC和I-PC的结合率分别为17.2±3.2%和11.6±2.5%（添加统计分析）。添加统计分析！ 是的 图1C 是的 图1C（a和b）显示了pH值为3.0的2 M尿素/HCl的结果。即使使用这种更有效的离解溶剂，天然I-AC和变性I-AC的27.1±3.5%和17.0±2.3%，±固定在柱上（表1）。这一差异表明，相当数量（17–27%）的I-AC分子可以与TiO2相连接，在这种更稳定的解离条件下，与I-PC结合的胶原蛋白百分比明显高于天然和变性形式的40.8±3.5%和24.1±2.3%±的比例。 是的 我们注意到，对于所有的天然胶原蛋白，一些尾随峰和通过峰，但与变性胶原，这些是没有观察到的（图。只有阿拉才知道这些字母的意义。 是的 表1 是的 ↑表1总结了在三种不同溶剂中，各种胶原蛋白与Ti结合百分比的百分比，共有六类：酸溶性胶原蛋白（AC）、胃蛋白酶溶解性胶原蛋白（PC），这两种类型都包括天然胶原蛋白和变性胶原蛋白，我们用三种不同的溶剂将每种胶原蛋白烧焦溶剂：稀HCl、2M尿素/PBS、2M尿素/HCl（pH 3.0）。图中所示为结合组分（用0.025 M NaOH洗脱峰）的色谱面积与所用样品总面积（通过部分和结合部分的总和）的比率（%s），这与Ti结合每种胶原蛋白的能力的强度相对应 4-2↓P13，L13~P15，L2.）。 用三种不同溶剂作为洗脱剂，其色谱曲线的结果似乎没有本质区别。然而，我们发现热变性前后通过率和洗脱峰的比率（结合比）存在显著差异。以天然胃蛋白酶溶性胶原（I-PC）为例，我们发现在2m尿素（ph3.0）中，结合率最高为40.8±3.5%，而Ti结合率在热变性后降至24.1±2.3%。 ¾调整大小 最有趣的是，变性后钛结合率降低。这些变化发生在所有三种溶剂下分析的所有胶原蛋白中，而不考虑端肽的存在。，Aas汇总在表1中，。。。T和图2，我们首次表明，这是在稀释HCl（pH.4.0）、2 M尿素（pH 7.4）和2 M尿素/HCl（pH 3.0）中，I型胶原可与TiO2结合的第一个证据。很明显，在胶原和变性后，Ti结合率降低到约2/3。Wwe在I-AC和I-PC中变性后，Ti结合率的降低趋势相同，如图2和表1所示。在pH值为4.0.0的尿素溶液中（pH值为2.30，pH值为4.0.M）时，在pH值为4.0.M的尿素溶液中变性。在ph4.0（HCl）、ph7.4（2m尿素）和ph3.0（2m尿素）中，变性后这些Ti结合率分别降低到19.3%、17.3%和17.0%。Student检验显示，三种不同溶剂的p值分别为0.003、0.0015和0.028，均具有统计学意义。 注释=4-2↓P13，L13~P15，L2-4°Dis to Res} 结果表明，在pH.4.0（HCl）、ph7.4（2m尿素）、ph3.0（2m尿素）、ph3.0（2m尿素）和ph3.0（2m尿素）条件下，变性前，I-PC与Ti柱的结合率分别为32.2%、25.9%和40.8%。但是，变性后，在上述溶剂中，这些结合比降低到20.6%、11.6%和24.1%（图2和表1）。↑以上三段（2/4-2、2/4-3和2/4-4）从Dis移到Res（在铬酸盐会议结束时）；）不要重复添加 STATI®-52-4/4° 对于端肽功能性要求在结合中的重要性，我们通过比较不同溶剂中I-AC和PC的色谱图，得到了明确的信息。。。当我们使用稀盐酸（ph4.0）作为溶剂时，I-AC（30.4%）和PC（32.2%）之间的Ti结合率没有显著差异（p:0.56）。变性胶原的差异要小得多，I-AC组为19.3%，I-PC组为20.6%（p:0.72）。然而，在灾难中

正在翻译中..

其它语言

本翻译工具支持: 世界语, 丹麦语, 乌克兰语, 乌兹别克语, 乌尔都语, 亚美尼亚语, 伊博语, 俄语, 保加利亚语, 信德语, 修纳语, 僧伽罗语, 克林贡语, 克罗地亚语, 冰岛语, 加利西亚语, 加泰罗尼亚语, 匈牙利语, 南非祖鲁语, 南非科萨语, 卡纳达语, 卢旺达语, 卢森堡语, 印地语, 印尼巽他语, 印尼爪哇语, 印尼语, 古吉拉特语, 吉尔吉斯语, 哈萨克语, 土库曼语, 土耳其语, 塔吉克语, 塞尔维亚语, 塞索托语, 夏威夷语, 奥利亚语, 威尔士语, 孟加拉语, 宿务语, 尼泊尔语, 巴斯克语, 布尔语(南非荷兰语), 希伯来语, 希腊语, 库尔德语, 弗里西语, 德语, 意大利语, 意第绪语, 拉丁语, 拉脱维亚语, 挪威语, 捷克语, 斯洛伐克语, 斯洛文尼亚语, 斯瓦希里语, 旁遮普语, 日语, 普什图语, 格鲁吉亚语, 毛利语, 法语, 波兰语, 波斯尼亚语, 波斯语, 泰卢固语, 泰米尔语, 泰语, 海地克里奥尔语, 爱尔兰语, 爱沙尼亚语, 瑞典语, 白俄罗斯语, 科西嘉语, 立陶宛语, 简体中文, 索马里语, 繁体中文, 约鲁巴语, 维吾尔语, 缅甸语, 罗马尼亚语, 老挝语, 自动识别, 芬兰语, 苏格兰盖尔语, 苗语, 英语, 荷兰语, 菲律宾语, 萨摩亚语, 葡萄牙语, 蒙古语, 西班牙语, 豪萨语, 越南语, 阿塞拜疆语, 阿姆哈拉语, 阿尔巴尼亚语, 阿拉伯语, 鞑靼语, 韩语, 马其顿语, 马尔加什语, 马拉地语, 马拉雅拉姆语, 马来语, 马耳他语, 高棉语, 齐切瓦语, 等语言的翻译.