Ostolovskiĭ E M, Botsianskiĭ A D, Zadorozhnyĭ B A
Biofizika. 1990 Sep-Oct;35(5):762-4.
Some intramolecular peculiarities of the structure of the blood albumin serum of some mammals were studied by means of probe luminescence polarization, phase fluorimetry, and solubilization. It has been shown that microviscosity of the "universal" hydrophobic nucleus where N-phenylnaphtylamine is localized is much above that in the surface regions of the protein globule filled with the probe I-anilinonaphtalene-8-sulphonate (ANS). High values of microviscosity of universal nuclei and surface hydrophobic regions were found in the albumins of man and guinea pig. In protein molecules of rabbit and bull lower microviscosity of probe surroundings was recorded both for the nucleus and peripheral surface regions. Rat albumin had higher microviscosity of ANS localization sites, while the density of the hydrophobic nucleus was comparatively low. At the same time an opposite phenomenon was observed in pig albumin preparations.
通过探针发光偏振、相荧光测定法和增溶作用研究了某些哺乳动物血清白蛋白结构的一些分子内特性。结果表明，N-苯基萘胺所在的“通用”疏水核的微粘度远高于充满探针I-苯胺基萘-8-磺酸盐（ANS）的蛋白质球体表面区域的微粘度。在人和豚鼠的白蛋白中发现了通用核和表面疏水区域的高微粘度值。在兔和牛的蛋白质分子中，无论是核区域还是外周表面区域，探针周围环境的微粘度都较低。大鼠白蛋白中ANS定位位点的微粘度较高，而疏水核的密度相对较低。同时，在猪白蛋白制剂中观察到了相反的现象。
