Biglycan and decorin bind close to the n-terminal region of the collagen VI triple helix.

The binding of native biglycan and decorin to pepsin-extracted collagen VI from human placenta was examined by solid phase assay and by measurement of surface plasmon resonance in the BIAcore(TM)2000 system. Both proteoglycans exhibited a strong affinity for collagen VI with dissociation constants (K(D)) of approximately 30 nm. Removal of the glycosaminoglycan chains by chondroitinase ABC digestion did not significantly affect binding. In coprecipitation experiments, biglycan and decorin bound to collagen VI and equally competed with the other, suggesting that biglycan and decorin bind to the same binding site on collagen VI. This was confirmed by electron microscopy after negative staining of complexes between gold-labeled proteoglycans and collagen VI, demonstrating that both biglycan and decorin bound exclusively to a domain close to the interface between the N terminus of the triple helical region and the following globular domain. In solid phase assay using recombinant collagen VI fragments, it was shown that the alpha2(VI) chain probably plays a role in the interaction.

Structure of ribosomal protein L30 from Thermus thermophilus at 1.9 A resolution: conformational flexibility of the molecule.

The crystal structure of ribosomal protein L30 from the extreme thermophilic bacterium Thermus thermophilus has been determined at 1. 9 A resolution. The crystals are trigonal and belong to space group P3(2)21, with unit-cell parameters a = b = 63.5, c = 77.8 A, alpha = beta = 90, gamma = 120 degrees and two molecules per asymmetric unit. The structure was solved by the molecular-replacement method with AMoRe and refined with X-PLOR to an R value of 20.3% and an R(free) of 25.3% in the resolution range 8-1.9 A. Detailed analyses of the structures of the two molecules in the asymmetric unit and comparison of T. thermophilus L30 structure with the structure of homologous L30 from Bacillus stearothermophilus reveal two flexible regions at opposite ends of the rather elongated molecule. Such flexibility could be important for the protein fitting in the ribosome. A comparison with B. stearothermophilus L30 shows a higher number of salt bridges and unbound positively charged residues and an increased accessible hydrophobic area on the surface of T. thermophilus L30. This could contribute to the stability of both the extreme thermophile protein and the ribosome as a whole.

Structural studies of ribosomal proteins.

Crystal and solution structures of fourteen ribosomal proteins from thermophilic bacteria have been determined during the last decade. This paper reviews structural studies of ribosomal proteins from Thermus thermophilus carried out at the Institute of Protein Research (Pushchino, Russia) in collaboration with the University of Lund (Lund, Sweden) and the Center of Structural Biochemistry (Karolinska Institute, Huddinge, Sweden). New experimental data on the crystal structure of the ribosomal protein L30 from T. thermophilus are also included.

Overexpression of the gene of ribosomal protein L30 from Thermus thermophilus and crystallization of the recombinant protein.

Ribosomal protein L30 from Thermus thermophilus was overexpressed in E. coli cells. The recombinant protein was isolated and crystallized. The crystals belong to the spatial group P3(1) 12, and their crystallographic parameters are not different from those of crystals obtained earlier from the ribosomal protein isolated from T. thermophilus.

[The effect of acute alcoholic intoxication on the morphofunctional properties of the peripheral blood erythrocytes]. / Vliianie ostroi alkogol'noi intoksikatsii na morfofunktsional'nye svoistva éritrotsitov perifericheskoi krovi.

In experiments on rabbits it has been established that the acute alcoholization causes prolonged uncompensated alterations of such physical and chemical properties of erythrocytes as the average volume, the concentration of dry substance and water, the density, the content of endoerythrocytal hemoglobin, as well as the concentration of erythrocytes and hemoglobin in blood.

[Characteristics of physico-chemical properties of circulating erythrocytes in the post-anoxia period]. / Kharakteristika fiziko-khimicheskikh svoistv tsirkuliruiushchikh éritrotsitov v postgipoksicheskii period.

The normobarometric hypoxic hypoxia stimulates different alterations in the fundamental parameters of physicochemical properties of the peripheric blood erythrocytes and has a stimulating effect on the system of the erythropoiesis in post-hypoxia period.

[Methods of analyzing hematologic characteristics based on light scattering]. / Metody analiza gematologicheskikh kharakteristik, osnovannye na svetorasseianii.

The methods of simultaneous identification of hematological blood parameters are described, i.e. general hemoglobin concentration, relative concentrations of hemoglobin derivatives, erythrocyte volume concentration, some erythrocyte aggregational parameters, checked on the same methodological basis. The tests were carried out on the banked blood samples. Their authenticity and accuracy are proved by the data derived from other independent methods. The preference of the offered approaches used for blood parameters tests compared to the ones presently used are being discussed.