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Structural changes in cod myosin after modification with formaldehyde or frozen storage

机译:甲醛改性或冷冻保存后鳕鱼肌球蛋白的结构变化

摘要

Structural changes in cod myosin after formaldehyde (FA) addition with and without subsequent freezing at - 18°C were examined by Raman spectroscopy, ANS hydrophobicity, solubility and SDS-PAGE profiles. Protein solubility decreased by >90%, whereas ANS fluorescence showed little change, possibly due to a balance between soluble and insoluble fractions differing in exposed hydrophobicity. SDS-PAGE showed irreversible insolubilization at increasing FA concentration, especially after frozen storage. Raman spectral analysis indicated a change in secondary structure of aquacide concentrated myosin preparations, from 95% α-helix in the control (no FA) to 60% after 12 mM FA treatment. Changes in vibrational modes assigned to aliphatic residues suggested involvement of hydrophobic interactions after FA addition or frozen storage.
机译:通过拉曼光谱,ANS疏水性,溶解度和SDS-PAGE曲线检查了添加和未添加甲醛后(FA)在18°C下冷冻后鳕鱼肌球蛋白的结构变化。蛋白质溶解度降低了> 90%,而ANS荧光显示的变化很小,这可能是由于暴露的疏水性不同的可溶性部分和不溶部分之间的平衡所致。 SDS-PAGE在FA浓度增加时表现出不可逆的增溶作用,尤其是在冷冻保存后。拉曼光谱分析表明,浓缩aquacide的肌球蛋白制剂二级结构发生了变化,从对照组的95%α-螺旋(无FA)到12mM FA处理后的60%。分配给脂肪族残基的振动模式的变化表明,添加FA或冷冻储存后,疏水相互作用会参与其中。

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  • 作者

    Careche Mercedes; Li-Chan E;

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  • 年度 2014
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  • 原文格式 PDF
  • 正文语种 eng
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