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We investigated wild-growing grassy plants such as Alhagi pseudalhagi, Zygophyllum, Juncus acutus and Argusia sibirica with the purpose of studying the mechanism of carry of radionuclides from ground in plants and an establishment most the common laws of distribution of radionuclides between different organs of plants. The results of the research show that the researched plants are mainly accumulated 40K. On a degree of accumulation, 226Ra occupies the second place, but 232Th doesn't participate almost in processes of carry from ground in plants. It is established that root systems of plants possesses unequal ability to absorb same radionuclides from the same ground. For example, the root system of Argusia sibirica is characterized by smaller ability to absorb 226Ra, but 40K is more accessible. It is shown that biological availability radionuclides in the given ground depends both on a kind of plants and on radionuclides. For example, Argusia sibirica, Zygophyllum show higher accumulating ability to 40K and in relation to 226Ra, Alhagi pseudalhagi and Juncus acutus are more sensitive. It is established that accumulating ability of stalks of different plants in relation to 40K are appreciably different. Distribution of radionuclides in seeds of plants has other character. Thus Alhagi pseudalhagi in the seeds had also certain amount of 232Th, and leaves Argusia sibirica in comparison with Zygophyllum have a high degree of accumulation as for 40K, so for 226Ra.

To elucidate the natural fatty acids effect on the human serum albumin (HSA) structure a new method of tritium labelling was used. The main peculiarity of the method consists in the possibility to get information on the qualitative and quantitative amino acid composition of the surface layer of the protein globule at different conformational states of the globule. Defatted HSA was shown to be characterized a higher accessibility of Asx, Glx, Thr, Ser, Gly, Pro, Ile, Tyr residues while the other residues remain unchanged. Asx residues are characterized by the largest changes (about 8 folds). Full accessible protein surface during defatting increases from 39,000 to 48,000 A2. Fatty acids connected with albumin in the relation 1-3 moles/mol of protein are noted to be the factor increasing the globule compactness and stipulating for the conformational protein stability to warmth, urine and guanidine salts effect.

Accessible surfaces of the HSA molecule in N-, F- and B-forms were studied in the present work by tritium labelling method which allowed to obtain detailed information on N-F- and N-B-transitions. In was shown that the F-form in comparison top the N-form is characterized by more high accessibility of Ser, Ala, Ile, Tyr, Phe, His, Arg, Pro, Val and Phe residues and in the B-form Tyr, Ser, Arg, Gly, Ile, Phe and Pro residues turn to be highly accessible. Full accessible surfaces of protein molecule at N-F- and N-B-transitions increase respectively from 39,000 to 70,400 A2 and from 39,000 to 47,000 A2. Basing on the prevailing increase of hydrophobic residues accessibility it is supposed that the molecule expansion testifies the separation of the subunits forming the molecule.

Amino acids composing an accessible surface of lysozyme and human serum albumin (HSA) globules were determined by the total tritium labelling method. A good correlation between our data on the distribution of the tritium label for the lysozyme molecule and X-ray data on the tertiary structure for this macromolecule was received. Lysozyme was used as a standard for determining the accessible surface of the globule albumin. It was shown that the accessible surface of the albumin globule is substantially more hydrophobic (average accessible surface area of hydrophobic amino acids is 130 A2 in HSA and 20 A2 in lysozyme) than in lysozyme. The HSA molecule is characterized by high values of: the accessible surface area, the ratio of extended area to the folded one, and the surface roughness index. These data indicate that the HSA molecule is less compactly packed than lysozyme.