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bluelu1984金虫 (小有名气)
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40 个金币求翻译一语段
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The purpose of this study is to investigate the mechanism of protein stabilization by sugars in the solid state. That is, explore whether the stabilization is controlled by ‘‘glass dynamics’’ or by native structure preservation through ‘‘specific interaction’’ between sugars and protein. The IgG1 antibody (150 kD) and recombinant human serum albumin (rHSA) (65 kD) were formulated with sorbitol, trehalose, and sucrose. Degradation of lyophilized formulations was quantified using size exclusion (SEC) and ion-exchange chromatography (IEX). The secondary structure of the protein in these formulations was characterized using Fourier Transform Infrared (FTIR) spectroscopy. The molecular mobility, as measured by the stretched relaxation time (tb) was obtained by fitting the modified stretched exponential (MSE) equation to the calorimetric data from the Thermal Activity Monitor (TAM). Compared with sucrose and trehalose, sorbitol could only slightly protect the protein against aggregation and had no effect on chemical degradation. The chemical degradation and aggregation rates of the protein decreased when the weight ratio of sucrose to protein increased from 0 to 2:1. Storage stability of the proteins showed a reasonably good correlation with the degree of retention of native structure of protein during drying as measured by the spectral correlation coefficient for FTIR spectra. The plots of tb as a function of fraction of sucrose passed through a maximum at 1:1 weight ratio of sucrose to protein. That is, the molecular mobility did not correlate with the stability of protein at high levels of sucrose content. Although the glass transition appears to be an important parameter for stability, protein stabilization by sugars in the solid state cannot be wholly explained by the glass dynamics mechanism, at least as measured by tb. However, it is possible that the b-relaxations rather than the a-relaxations (i.e., the t we measured) are critical to stability. The data show that storage stability correlates best with ‘‘structure’’ as determined by FTIR spectroscopy. However, while a specific interaction between stabilizer and protein might be responsible for the preservation of native structure, the evidence supporting this position is not compelling. |
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bluelu1984
金虫 (小有名气)
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- 注册: 2009-01-09
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- 专业: 天然药物化学
2楼2009-04-07 20:45:21
仅供参考
★ ★ ★
bluelu1984(金币+3,VIP+0):翻译的很不准确 4-8 14:02
bluelu1984(金币+3,VIP+0):翻译的很不准确 4-8 14:02
| 本研究的目的是调查的机制，稳定的糖蛋白中的固体状态。也就是说，探讨是否稳定控制的动态'' ''玻璃或由天然结构保存通过具体互动'' ''之间糖和蛋白质。该IgG1抗体（ 150科威特第纳尔）和重组人血清白蛋白（重组人血清白蛋白） （ 65科威特第纳尔）制定了与山梨糖醇，海藻糖和蔗糖。冻干制剂降解是量化使用尺寸排阻（ SEC ）的和离子交换层析（ IEX ） 。二级结构的蛋白在这些配方特点是利用傅立叶变换红外光谱（ FTIR ）光谱。分子流动性，衡量的延伸弛豫时间（ TB ）的拟合，得到的修改扩展指数（微型和小型企业）方程的热数据热活性检测系统（谭） 。与蔗糖和海藻糖，山梨糖醇可能只是略有保护蛋白对聚集，并没有影响化学降解。化学退化和聚集率下降的蛋白质时，重量比蔗糖蛋白质从0提高到2:1 。贮存稳定性的蛋白质表现出良好的相关性与合理的程度保留天然结构干燥过程中的蛋白质来衡量的谱相关系数的红外光谱。情节结核病作为一个功能部分蔗糖通过最高重量比在1:1蔗糖蛋白质。也就是说，分子流动没有相关的蛋白质的稳定在高水平的蔗糖含量。虽然玻璃化转变似乎是一个重要参数的稳定，稳定的糖蛋白中的固态不能完全解释的玻璃动力学机制，至少作为衡量结核。然而，也有可能在B -放宽，而不是一个松弛（即吨我们衡量）是至关重要的稳定。数据显示，储存稳定性的相关性最好的结构与'' ''所确定的红外光谱。然而，尽管特定的稳定剂之间的相互作用和蛋白质可能是负责保存的天然结构，证据支持这一立场是不能令人信服的。 |
3楼2009-04-08 13:20:11
zj19820305
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4楼2009-04-08 13:53:14
zj19820305
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5楼2009-04-08 14:08:43
zj19820305
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6楼2009-04-08 14:27:25
zj19820305
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7楼2009-04-08 14:30:56