Hyperthermia (heat shock)-induced protein denaturation in liver, muscle and lens tissue as determined by differential scanning calorimetry.
Hyperthermia (heat shock)-induced protein denaturation in liver, muscle and lens tissue as determined by differential scanning calorimetry.
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DOI：
10.3109/02656739409022441
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发表时间：
1994-09
期刊：
影响因子：
--
通讯作者：
K. Ritchie;B. M. Keller;K. M. Syed;J. Lepock
中科院分区：
文献类型：
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作者：
K. Ritchie;B. M. Keller;K. M. Syed;J. Lepock
蛋白质变性已被证明发生在细胞在热休克，并密切相关的细胞对高温的反应，然而，很少有人知道在组织中的蛋白质变性。本研究采用差示扫描量热法（DSC）分析了Wistar大鼠、新西兰白色兔和虹鳟鱼肝脏、白色肌肉和透镜组织在高温区的吸热转变。获得了每个组织的复杂DSC曲线，包括几个转变。有证据表明，这些转变主要是由于蛋白质变性。大鼠肝脏、肌肉和透镜的变性起始温度（T1）分别为约38、39和48 ℃。因此，在轻度高温（40-45 ℃）期间，肝脏和肌肉中发生显著的蛋白质变性，其中透镜相当稳定。来自不同动物的相同组织的T1值与体温良好相关（兔39.4，大鼠38.2，和在11摄氏度下生长的鳟鱼）; T1以与每个组织的体温相同的顺序增加。因此，这些组织中蛋白质变性的起始温度与体温之间存在相关性。
Protein denaturation has been shown to occur in cells during heat shock and is closely correlated with the cellular responses to hyperthermia; however, little is known about protein denaturation in tissue. This study describes an analysis of endothermic transitions in the hyperthermic region using differential scanning calorimetry (DSC) in liver, white muscle, and lens tissue from Wistar rat, New Zealand white rabbit, and Rainbow trout. Complex DSC profiles consisting of several transitions were obtained for each tissue. Evidence is given that these transitions are due primarily to protein denaturation. Onset temperatures of denaturation (Tl) for rat liver, muscle, and lens are about 38, 39 and 48 degrees C, respectively. Thus, significant protein denaturation occurs in liver and muscle during mild hyperthermia (40-45 degrees C) with lens considerably more stable. The values of Tl for the same tissue from the different animals correlates well with body temperature (rabbit 39.4, rat 38.2, and trout grown at 11 degrees C); Tl increased in the same order as the body temperature for each tissue. Thus, there is correlation between the onset temperature for protein denaturation in these tissues and body temperature.