Ostolovskiĭ E M, Botsianskiĭ A D, Zadorozhnyĭ B A
Biofizika. 1988 Mar-Apr;33(2):356-8.
Some peculiarities of hydrophobic structure of serum albumine of some mammals were studied by NMR-spectroscopy, solubilization and fluorescent probes. It has been shown that the FNA probe is bound to the most hydrophobic cavities in the protein molecules, and the sizes of these regions in mammalian albumines are very close. The data obtained by ANS probe show that there exists a proportional relationship between the fluorescence intensity, the total volume of hydrophobic cavities and the quantity of "bound water". When using the ANS--Mg1/2 probe in all cases an increase of fluorescence intensity was obtained. It was concerned with the stabilizing effect of magnesium ions on the protein molecule.
通过核磁共振光谱法、增溶作用和荧光探针研究了一些哺乳动物血清白蛋白疏水结构的某些特性。结果表明，FNA探针与蛋白质分子中最疏水的腔结合，并且哺乳动物白蛋白中这些区域的大小非常接近。ANS探针获得的数据表明，荧光强度、疏水腔的总体积与“结合水”的量之间存在比例关系。在所有情况下，使用ANS-Mg1/2探针时荧光强度都会增加。这与镁离子对蛋白质分子的稳定作用有关。
