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首页> 外文期刊>Langmuir >Secondary Structural Changes of Homologous Proteins, Lysozyme and α?Lactalbumin, in Thermal Denaturation up to 130 °C and Sodium Dodecyl Sulfate (SDS) Effects on These Changes: Comparison of Thermal Stabilities of SDS-Induced Helical Structures in These Proteins
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Secondary Structural Changes of Homologous Proteins, Lysozyme and α?Lactalbumin, in Thermal Denaturation up to 130 °C and Sodium Dodecyl Sulfate (SDS) Effects on These Changes: Comparison of Thermal Stabilities of SDS-Induced Helical Structures in These Proteins

机译：同源蛋白，溶菌酶和α？乳清蛋白在高达130°C的热变性中的二级结构变化和十二烷基硫酸钠（SDS）对这些变化的影响：比较这些蛋白中SDS诱导的螺旋结构的热稳定性

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摘要

The thermal stability of two homologous proteins,nlysozyme and α-lactalbumin, was examined by circular dichroism.nThe present study clearly showed two different aspects betweennthe homologous proteins: (1) the original helices of lysozyme andnα-lactalbumin were unchanged at heat treatments up to 60 and 40n°C, respectively, indicating a higher thermal stability of lysozyme,nand (2) upon cooling to 25 °C, the original helices of lysozymenwere never reformed after they were once disrupted, while those ofnα-lactalbumin, disrupted at a particular temperature range betweenn40 and 60 °C, were completely reformed. In addition, thenstructural changes were also examined in the coexistence ofnsodium dodecyl sulfate (SDS), which induced the formation ofnhelical structures in these proteins at 25 °C. A distinct difference appeared in the thermal stabilities of the SDS-induced helices.nAll of the SDS-induced helices of lysozyme were disrupted below 60 °C, while those of α-lactalbumin at 10 mM SDS werenunchanged up to 130 °C. A similarity was also fixed. Not only the SDS-induced helices but also the original helices of the twonproteins were reformed upon cooling to 25 °C after the thermal denaturation below 100 °C in the coexistence of 10 mM SDS.
机译：通过圆二色性检测了两种同源蛋白，溶菌酶和α-乳白蛋白的热稳定性。分别为60和40n°C，表明溶菌酶的热稳定性更高，nand（2）冷却至25°C时，溶菌酶的原始螺旋一旦被破坏就不会再形成，而nα-乳白蛋白的螺旋则在特定温度下被破坏。温度范围完全在40至60°C之间。此外，还在十二烷基硫酸钠（SDS）的共存下检查了结构变化，该结构在25°C下诱导了这些蛋白质中的螺旋结构的形成。 SDS诱导的螺旋的热稳定性出现了明显的差异.n在60°C以下，所有SDS诱导的溶菌酶螺旋均被破坏，而在130 mC的温度下，在10 mM SDS下的α-乳清蛋白则未发生变化。相似性也已修复。在10 mM SDS共存下低于100°C进行热变性后，冷却至25°C时，不仅SDS诱导的螺旋也将重组twon蛋白的原始螺旋。

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  • 来源
    《Langmuir》 |2012年第47期|16268-16273|共6页
  • 作者

    Yoshiko Moriyama; Naoaki Kondo; and Kunio Takeda;

  • 作者单位

    Department of Applied Chemistry and Biotechnology Okayama University of Science 1-1 Ridai-cho Kita-ku Okayama 700-0005Japan;

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