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通过光谱法研究中-四(4-磺酸苯基)卟啉与血红素结合蛋白和白蛋白的结合情况。

Binding of meso-tetra(4-sulfonatophenyl)porphine to haemopexin and albumin studied by spectroscopy methods.

作者信息

Bartosová J, Kalousek I, Hrkal Z

机构信息

Department of Cell Biochemistry, Institute of Haematology and Blood Transfusion, Praha, Czech Republic.

出版信息

Int J Biochem. 1994 May;26(5):631-7. doi: 10.1016/0020-711x(94)90162-7.

Abstract
  1. The interaction of haemopexin and albumin with TPPS4 was studied by measuring the absorption and fluorescence spectra. Haemopexin was found to have one strong TPPS4 binding center (Ka = 3 x 10(7) M-1). 2. Haem-haemopexin complex appears to have no specific binding site for TPPS4. Occupation of the specific binding center of haemopexin molecule by a haem abolishes TPPS4 binding. 3. Albumin was found to possess one strong TPPS4 binding center (Ka = 3 x 10(6) M-1) besides two or three weak binding sites (Ka = 2 x 10(5) M-1). 4. Haem-albumin complex possesses only one weak TPPS4 binding site (Ka = 7 x 10(5) M-1). These observations suggest identity of primary binding sites of TPPS4 and haem on albumin molecule.
摘要
  1. 通过测量吸收光谱和荧光光谱研究了血红素结合蛋白和白蛋白与四苯基卟吩磺酸(TPPS4)的相互作用。发现血红素结合蛋白有一个强的TPPS4结合中心(Ka = 3×10⁷ M⁻¹)。2. 血红素 - 血红素结合蛋白复合物似乎没有TPPS4的特异性结合位点。血红素占据血红素结合蛋白分子的特异性结合中心会消除TPPS4的结合。3. 发现白蛋白除了有两三个弱结合位点(Ka = 2×10⁵ M⁻¹)外,还有一个强的TPPS4结合中心(Ka = 3×10⁶ M⁻¹)。4. 血红素 - 白蛋白复合物仅具有一个弱的TPPS4结合位点(Ka = 7×10⁵ M⁻¹)。这些观察结果表明TPPS4和血红素在白蛋白分子上的主要结合位点相同。

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