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脱辅基α-乳白蛋白处于熔球态时热转变的缺失。差示扫描微量热法研究

Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry.

作者信息

Yutani K, Ogasahara K, Kuwajima K

机构信息

Institute for Protein Research, Osaka University, Japan.

出版信息

J Mol Biol. 1992 Nov 20;228(2):347-50. doi: 10.1016/0022-2836(92)90824-4.

Abstract

To estimate the energy level of the molten globule state, the heat capacity function of apo-alpha-lactalbumin in the molten globule state has been examined using a scanning microcalorimeter at neutral pH. The results showed that the enthalpy difference between the molten globule state and presumed unfolded state by heating was almost zero at neutral pH, demonstrating that the molten globule state does not exhibit any co-operative transition upon heating. This is in agreement with the results already reported at acid pH, but is apparently in conflict with that recently reported with some assumptions at neutral pH.

摘要

为了估算熔球态的能量水平,已使用扫描微量热计在中性pH条件下检测了脱辅基α-乳白蛋白在熔球态下的热容函数。结果表明,在中性pH条件下,通过加热,熔球态与假定的未折叠态之间的焓差几乎为零,这表明熔球态在加热时不会出现任何协同转变。这与在酸性pH条件下已报道的结果一致,但显然与最近在中性pH条件下基于一些假设所报道的结果相矛盾。

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