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首页> 外文期刊>Journal of Undergraduate Chemistry Research >STUDIES ON THE EFFECTS OF OXIDATIVE MODIFICATIONS IN HUMAN SERUM ALBUMIN ON ITS INTERACTIONS WITH MAGNETIC IRON (III) OXIDE NANOPARTICLES
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STUDIES ON THE EFFECTS OF OXIDATIVE MODIFICATIONS IN HUMAN SERUM ALBUMIN ON ITS INTERACTIONS WITH MAGNETIC IRON (III) OXIDE NANOPARTICLES

机译:人体血清白蛋白氧化修饰作用及其与磁性氧化铁(III)纳米粒子相互作用的研究

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摘要

The effects of oxidative modifications in human serum albumin on its interactions with magnetic nanoparticles (MNP) were investigated using spectroscopic techniques. Results indicated that unoxidized albumin binds tightly with magnetic iron (!!!) oxide particles with a binding constant (K_a) of 1.06 (+0.08) x 10~6M~(-1). The circular dichroism spectra suggested that the addition of MNP caused mild changes in the secondary structure of the protein. Metal catalyzed oxidation (MCO) of human serum albumin significantly affected its binding affinity with MNP. After 2 hours of oxidation, the binding constant (K_a) of the fibrinogen-MNP interaction showed a five-fold decrease compared to that of unoxidized protein.
机译:使用光谱技术研究了人血清白蛋白中氧化修饰对其与磁性纳米颗粒(MNP)相互作用的影响。结果表明,未氧化的白蛋白与磁性氧化铁颗粒紧密结合,结合常数(K_a)为1.06(+0.08)x 10〜6M〜(-1)。圆二色性光谱表明,添加MNP会引起蛋白质二级结构的轻微变化。人血清白蛋白的金属催化氧化(MCO)显着影响其与MNP的结合亲和力。氧化2小时后,与未氧化蛋白相比,血纤蛋白原与MNP相互作用的结合常数(K_a)降低了五倍。

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