[Intramolecular structure of mammalian serum albumin].

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.

[Study of the structure of mammalian serum albumin using fluorescent probes].

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".