Temperature and pH Effect on the Polymorphism of Aprotinin (BPTI) in Sodium Bromide Solutions
Temperature and pH Effect on the Polymorphism of Aprotinin (BPTI) in Sodium Bromide Solutions
复制标题
温度和 pH 对溴化钠溶液中抑肽酶 (BPTI) 多态性的影响
DOI：
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发表时间：
2004
期刊：
影响因子：
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通讯作者：
J. Astier
中科院分区：
文献类型：
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作者：
S. Veesler;N. Ferté;Marie;M. Czjzek;J. Astier
在这方面的贡献，我们提出了作为温度和pH值的函数的蛋白质晶体在悬浮液中的相变。我们测量的溶解度的抑肽酶（BPTI）的两种多晶型物在2 M NaBr溶液中在不同的酸性pH值之间的4.50和5.13在20 °C。当pH从4.5增加到5.13时，我们观察到溶解度的显著增加。在pH 4.5和4.75下研究了5至35 °C之间的温度对两种BPTI多晶型物在2M NaBr溶液中的溶解度的影响。我们通过直接和反向溶解度曲线观察到同一溶液中的两种多晶型物。我们表明，在两种多晶型物之间的转变温度附近的温度的适当控制可用于获得所需的多晶型物。
In this contribution, we present the phase transition of protein crystals in suspension as a function of temperature and pH. We measure the solubility of two polymorphs of aprotinin (BPTI) in 2 M NaBr solutions at different acidic pH values between 4.50 and 5.13 at 20 °C. We observe a major increase in solubility when the pH is increased from 4.5 to 5.13. The temperature effect between 5 and 35 °C on the solubility of the two BPTI polymorphs in 2 M NaBr solutions is investigated at pH 4.5 and 4.75. We observe two polymorphs in the same solution with direct and reverse solubility curves. We show that an adequate control of temperature around the transition temperature between the two polymorphs can be used to obtain the polymorph desired.