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

International Journal of Biochemistry Pub Date : 1994-05-01 Epub Date: 2003-02-05 DOI:10.1016/0020-711X(94)90162-7

J. Bartošová, I. Kalousek, Z. Hrkal

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引用次数: 16

Abstract

1.
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 (K_a = 3 × 10⁷M⁻¹).
2.
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.
3. Albumin was found to possess one strong TPPS₄ binding center (K_a = 3 × 10⁶M⁻¹) besides two or three weak binding sites (K_a = 2 × 10⁵M⁻¹).
4.
4. Haern-albumin complex possesses only one weak TPPS₄ binding site (K_a = 7 × lO⁵M⁻¹). These observations suggest identity of primary binding sites of TPPS₄ and haem on albumin molecule.

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用光谱学方法研究了中四(4-磺酰基)卟啉与血红素和白蛋白的结合

1.1. 通过吸收光谱和荧光光谱研究血红素和白蛋白与TPPS4的相互作用。血氧蛋白具有一个较强的TPPS4结合中心(Ka = 3 × 107M−1)。血氧蛋白复合物似乎对TPPS4没有特异性的结合位点。血红素占领血凝素分子的特异性结合中心可消除TPPS4的结合。白蛋白除了具有两个或三个弱结合位点(Ka = 2 × 105M−1)外，还具有一个强TPPS4结合中心(Ka = 3 × 106M−1)。haern -白蛋白复合物仅具有一个弱TPPS4结合位点(Ka = 7 × lO5M−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是相同的。

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International Journal of Biochemistry

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