应激抗性蛋白对应激敏感蛋白的非特异性稳定作用：热休克蛋白生物学作用的一种模型。
Nonspecific stabilization of stress-susceptible proteins by stress-resistant proteins: a model for the biological role of heat shock proteins.
作者信息
Minton K W, Karmin P, Hahn G M, Minton A P
出版信息
Proc Natl Acad Sci U S A. 1982 Dec;79(23):7107-11. doi: 10.1073/pnas.79.23.7107.
Abstract
It is demonstrated experimentally that addition of proteins that are themselves resistant to denaturation by heat or ethanol can nonspecifically stabilize other proteins that are ordinarily highly susceptible to inactivation. It is proposed that the diffusion-limited rate with which unfolded protein molecules encounter each other and become irreversibly crosslinked is reduced in the presence of substantial concentrations of an unreactive globular protein. We suggest that one of the functions of heat shock proteins, which are synthesized in large amounts after exposure of cells to increased temperature and other forms of stress, may be to stabilize other proteins kinetically in a similarly nonspecific fashion.
摘要
实验证明，添加本身对热或乙醇变性具有抗性的蛋白质可以非特异性地稳定其他通常极易失活的蛋白质。有人提出，在存在大量无反应性球状蛋白质的情况下，未折叠的蛋白质分子相互碰撞并不可逆交联的扩散限制速率会降低。我们认为，热休克蛋白的功能之一，即在细胞暴露于升高的温度和其他形式的应激后大量合成的蛋白质，可能是以类似的非特异性方式在动力学上稳定其他蛋白质。
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本文引用的文献
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Similarities in cellular inactivation by hyperthermia or by ethanol.热疗或乙醇导致细胞失活的相似性。
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Antibodies to two major chicken heat shock proteins cross-react with similar proteins in widely divergent species.针对两种主要鸡热休克蛋白的抗体与广泛不同物种中的相似蛋白发生交叉反应。
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