In situ spectroscopic quantification of protein-ice interactions.

In situ spectroscopic quantification of protein-ice interactions.
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DOI:
10.1021/jp403267x
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发表时间:
2013-07-03
期刊:
The journal of physical chemistry. B
影响因子:
--
通讯作者:
Aksan A
Aksan A
中科院分区:
其他
文献类型:
--
作者:
Twomey A;Less R;Kurata K;Takamatsu H;Aksan A

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利用傅里叶变换红外光谱和共聚焦拉曼光谱研究了在二甲基亚砜(DMSO)溶液中准平衡冻结过程中白蛋白与冰的相互作用。在−4和−6℃的温度下,在近平衡冻结过程中,白蛋白优先被排除在冰相之外。在较低的温度下,这种行为发生了逆转。取而代之的是,DMSO优先被排除在冰相之外,导致冷冻浓缩液体中的白蛋白浓度低于预期。据推测,这是由于冷冻浓缩液体中的白蛋白被吸附到冰面上或被困在冰相中造成的。观察到,在某些冷冻条件下,起始浓度为32-53 mg/mL的溶液中多达20%的白蛋白可能被吸附到冰界面上或被包裹在冰相中。
FTIR and confocal Raman microspectroscopy were used to measure interactions between albumin and ice in situ during quasi-equilibrium freezing in dimethyl sulfoxide (DMSO) solutions. At temperatures of −4 and −6 °C, albumin was found to be preferentially excluded from the ice phase during near-equilibrium freezing. This behavior reversed at lower temperatures. Instead, DMSO was preferentially excluded from the ice phase, resulting in an albumin concentration in the freeze-concentrated liquid phase that was lower than predicted. It is hypothesized that this was caused by the albumin in the freeze-concentrated liquid getting adsorbed onto the ice surface or becoming entrapped in the ice phase. It was observed that, under certain freezing protocols, as much as 20% of the albumin in solutions with starting concentrations of 32–53 mg/mL may be adsorbed onto the ice interface or entrapped in the ice phase.
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发表时间: 1998-09-01
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