COMPARISON OF METHYL VIOLET INTERACTION WITH BOVINE SERUM ALBUMIN AND HUMAN SERUM ALBUMIN BY UV-DENATURATION METHOD

M. Shahinyan, M. Mikaelyan, M. Parsadanyan, A. Antonyan
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Abstract

In the present work the interaction of methyl violet (MV) with human serum albumin (HSA) and bovine serum albumin (BSA) has been studied by the UV-denaturation method and the obtained data were compared. The denaturation parameters – denaturation temperature and denaturation interval width, were determined. It was shown that MV, binding to serum albumins, stabilizes their structure. At the same time, the stabilization degree is different. It was also shown that BSA is stabilized more, than HSA, while binding to MV.
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用紫外变性法比较甲基紫与牛血清白蛋白和人血清白蛋白的相互作用
本文用紫外变性法研究了甲基紫(MV)与人血清白蛋白(HSA)和牛血清白蛋白(BSA)的相互作用,并对所得数据进行了比较。确定了变性参数——变性温度和变性区间宽度。结果表明,MV与血清白蛋白结合,稳定其结构。同时,稳定化程度不同。结果表明,在与MV结合时,BSA比HSA更稳定。
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