首页> 外文期刊>Journal of Dairy Research >Pressure denaturation and aggregation of β-lactoglobulin studied by intrinsic fluorescence depolarization, Rayleigh scattering, radiationless energy transfer and hydrophobic fluoroprobing
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Pressure denaturation and aggregation of β-lactoglobulin studied by intrinsic fluorescence depolarization, Rayleigh scattering, radiationless energy transfer and hydrophobic fluoroprobing

机译:通过固有荧光去极化,瑞利散射,无辐射能量转移和疏水性氟探测研究β-乳球蛋白的压力变性和聚集

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摘要

β-Lactoglobulin (β-lg) in aqueous solution under pressure showed a marked depolarization of intrinsic fluorescence assigned to a gradually increased rotational diffusion of tryptophyl moieties in pressure-unfolded states. The corresponding change in anisotropy provided a new and more accurate method for determining denaturation volume which, for β-lg in neutral aqueous solution with ionic strength 0.16 (NaCl) at 25 deg. C, was ΔV=-73 (SE3) ml mol~-1, corresponding to half denaturation at 123 Mpa.
机译:压力下水溶液中的β-乳球蛋白(β-lg)表现出固有荧光的显着去极化,这与色氨酸部分在压力展开状态下的旋转扩散逐渐增加有关。各向异性的相应变化提供了一种新的更准确的测定变性体积的方法,该方法对于25度离子强度为0.16(NaCl)的中性水溶液中的β-Ig。 C为ΔV= -73(SE 3)ml mol -1,对应于123Mpa下的半变性。

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