牛α - s-酪蛋白的结构

K. Shimazaki, S. Sugai, R. Niki, S. Arima
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引用次数: 0

摘要

采用红外光谱法和旋光色散法研究了牛α - s-酪蛋白和化学修饰的α - s-酪蛋白在不同溶剂中的二级结构。α - s-酪蛋白的氨基被琥珀化或乙酰化,羧基被甲基化或乙基化。乙酰化和乙基化的-α - s酪蛋白不溶于水。水溶性样品在水中具有无序结构。在有机溶剂中,如2-氯乙醇和乙二醇,它们的α-螺旋分数约为50%。另一方面,甲基化的-α - s-酪蛋白在d20 - ch3od混合溶剂中有两个以1625和1643 cm−1为中心的红外吸收峰。这一事实可能与β结构的存在有关。在含有CH3OH的溶液中铸造的固体薄膜中,也发现了β结构的存在。作者试图从甲基化-α -s -酪蛋白的静电相互作用来解释甲基化-α -s -酪蛋白β-结构的形成。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Structure of Bovine αs-Casein
The secondary structure of bovine αs-casein and chemically modified αs-casein in various solvents was investigated by infrared absorption spectrum and optical rotatory dispersion measurements. Amino groups of αs-casein were either succinylated or acetylated, and carboxyl groups were either methylated or ethylated. Acetylated- and ethylated-αs-caseins are insoluble in water. Water-soluble samples have unordered structure in water. In organic solvents, such as 2-chloroethanol and ethylene glycol, they have about 50% α-helical fraction. On the other hand, it was found that methylated-αs-casein had two infrared absorption peaks centered at 1625 and 1643 cm−1 in D2O-CH3OD mixed solvent. This fact may be connected with the presence of β-structure. In the case of solid film of this sample, cast from solution containing CH3OH, the presence of β-structure was indicated, too. The authors attempted to explain the formation of β-structure in methylated-αs-casein in terms of the electrostatic interactions due to the d...
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