Phenolic profile of Potentilla anserina L. (Rosaceae) herb of siberian origin and development of a rapid method for simultaneous determination of major Phenolics in P. anserina pharmaceutical products by microcolumn RP-HPLC-UV.

A chemical study of Potentilla anserina L. herb (Rosaceae) of Siberian origin led to the isolation of 17 compounds. Three ellagitannins-potentillin, agrimonic acid A and B-are reported for the first time in this species.

[Clinical and immunogenetic aspects of children with local and multiple forms of primary tuberculosis].

Immunogenetic examination of 146 preschool children with local and multiple tuberculous lesions and 148 controls found out the key role of unfavourable premorbid background (low-quality BCG vaccine, family contacts, associated diseases) in the disease onset. General trends in systemic immunity shifts are characterized. These depend on the age, inflammation phase, severity of clinical symptoms.

[Erythrocyte aggregation in the blood in different states of the animal organism].

Aggregation of erythrocytes in the blood of rabbits was shown to depend on concentration of proteoglycans in the blood plasma. In experimental sepsis (Str. haemolyticus) there occurred simultaneous increase of concentration of proteoglycans in plasma and increased aggregation of erythrocytes in the blood.

[Action of proteoglycans on erythrocytes in circulating blood].

Rabbit and mice were injected into the blood stream sodium hyaluronate (0.1 mg per 1 g of the body animal) and protein-chondroitin-keratan-sulfate sodium (0.2 mg per 1 g of the body animal) in 0.

[The mechanism of the steric exclusion of cells brought about by proteoglycans].

The effect of amount of rabbit erythrocytes and concentration of sodium hyaluronate and sodium salt of protein--chondroitin-keratan-sulfate were studied on aggregation of erythrocytes suspended in 0.15 M NaCL, pH 7.4.

[Study of tissue proteoglycans by means of infrared spectroscopy].

The infrared spectra of the hyalin cartilage vitreous body, cornea, sclera and spectra of standard normal Na(+)-salts of hyaluronic acid, chondroitin-4-sulfate, chondroitin-6-sulfate, protein-chondroitin-keratan-sulfate, aggregates of proteoglycans of the hyalin cartilage, heparin fractions containing 3 and 4 residues of sulfuric acid per dimer of polymer were obtained. The comparative analysis of the spectra for tissues and of the spectra for proteoglycans made it possible to identify different proteoglycans in the same tissues.

[Protein motifs and their structure-functional role].

The review deals with repeating fragments of amino acid sequences, so-called "motifs", that are important in maintaining structural integrity and/or function of various proteins, especially those interacting with phospholipid aggregates. The occurrence of Phe-Leu-Gly motif characteristic for the amino acid sequence of the primate immuno-deficiency viruses fusion peptides is analysed in various proteins, as well as tripeptide fragments of general formula Xaa-Xah-Gly (Xaa-Phe, Tyr; Xab-hydrophobic amino acids Ala, Val, Leu, Ile) homologous to the above motif and retro-sequences Gly-Xab-Xaa. These tripeptide repeats are characteristic for the amino acid sequences of complex membrane proteins, viral envelope proteins, proteinases and proteins connected with energy transfer or interacting with lipids.

[The comparative study of the IR spectra of proteoglycans].

The IR spectra of sodium salt hyaluronic acid, chondroitin-4-sulfate, chondroitin-6-sulfate, dermatan-sulfate, protein-chondroitin-keratan-sulfate and aggregates of proteoglycans of the hyaline cartilage, heparin fractions containing 3 and 4 residues of sulfuric acid per dimer of polymer were obtained. It was shown that comparative analysis of IR spectra of the proteoglycans makes it possible to identify the 1150 cm-1, 1125 cm-1.

[Study of eye proteoglycans by means of infrared spectroscopy].

The infrared spectra of standard hyaluronic acid, proteochondroitin sulfate, aggregates of proteoglycans and spectra of the vitreous body, cornea and sclera were obtained in the region of 4000-400 cm-1. The comparative analysis of the spectra of these tissues and spectra made it possible to identify greater absorption bands of these biopolymers.

[Electron microscopic study of various salts of proteoglycan aggregates].

Chemically isolated preparations of acid and normal Mg2+, Ca2+-, and guanidine+ salts of cartilage proteoglycan aggregates were investigated by electron microscopy. Some differences between acid and normal salts depend on the amount, valency and distribution of basic ion as well as between carboxyl and sulphate groups.

[The role of different proteoglycan salts as factors in steric exclusion].

It has been shown that the capacity of Ca2+ salts of hyaluronic acid (HA) and nonaggregating protein-chondroitin-keratan-sulfate (PCKS) to divide in erythrocyte-saline suspension into liquid and cell phases was stronger than the analogous capacity of K+ salts. It was suggested that this is connected with a tendency to form different three-dimensional structures in solutions, which was more expressed in HA and PCKS Ca2+ salts than in K+ salts of these proteoglycans.

[Study of articular cartilage and the synovial membrane using IR spectroscopy].

The infrared spectra of normal knee joint cartilage, normal and rheumatoid arthritis-affected human synovial membrane and the same normal bovine tissues were obtained over the region of 400--4000 cm-1. A comparative analysis of the spectra of these tissues and those containing hyaluronate, protein-chondroitin-keratan sulfate aggregates of cartilage proteoglycans and heparin made it possible to identify greater absorption bands of these biopolymers in the tissue spectra. The interpretation of the results obtained is presented.

[Effect of actinomycin D, cycloheximide, puromycin and mitomycin C on the biosynthesis of heat shock proteins in the nuclear matrix of Chinese hamster fibroblasts].

The thermal shock proteins with molecular mass of 86 kD and pI 5.5 as well as of 70 kD and pI 5.2-5.

[Role of heparin in erythrocyte aggregation].

The effect of two heparin fractions containing 3 (HP-3) and 4 (HP-4) residues of sulfuric acid per dimer of polymers on the capacity of hyaluronate potassium (HUP) and protein-chondroitin-keratan-sulfate potassium (PCHKSP) to aggregate rabbit erythrocytes suspended in 0.15 M NaCl was studied. HP-3 (0.

[Interaction of proteoglycans with proteins].

The method has been developed for preparing complexes of lysozyme with chondroitin sulfate-4 and -6, non-aggregated (soluble) proteoglycans, cartilage proteoglycan aggregates, heparin fractions containing residues 3(H-3) and 4(H-4) of sulfuric acid per dimer of polymer. The studies of the chemical composition and IK-spectra of proteoglycan-lysozyme complexes have demonstrated the electrostatic nature of proteoglycan-lysozyme interaction.

[Heat-shock proteins in the nuclear matrix of Chinese hamster fibroblasts].

Heating of Chinese hamster fibroblasts (46 degrees C, 10 min) results in sharp inhibition of protein biosynthesis in the homogenate, nuclei and, in a lesser degree, in the nuclear matrix. The ratio of specific radioactivity of nuclear matrix 35S-proteins to the homogenate radioactivity taken for 100% increases after the heat shock 2,5-fold. Thus, protein biosynthesis in the nuclear matrix is more stable to the damaging action of heat shock than that in the homogenate and nuclei.

[Biological role of hyaluronic acid (review)].

The most important studies on hyaluronic acid carried out within the recent 5-7 years are reviewed. Chemical structure, physical parameters and properties of hyaluronic acid are considered. Various functions of hyaluronic acid are discussed on the basis of current information.

[Effect of hyperthermia on the polypeptide composition of the nuclear matrix of the rat liver].

The increase in rat body temperature by 2-3 degrees as a result of overheating (45 degrees C, 22% humidity) over 90 and 120 min is accompanied by changes in the rate of labeled precursors incorporation into rat liver protein fractions. The incorporation of labeled amino acids into liver nuclear matrix proteins within the first 90 min of overheating is somewhat decreased, whereas 120 min thereafter it exceeds by 30% the corresponding values in control animals kept at room temperature. The polypeptide pattern of the nuclear matrix in hyperthermia is characterized by an increased relative content of polypeptide components around Mr 100, 55, 40 and 30 kDa against a decreased level of several polypeptides as compared to the control.

[2 functions of proteoglycans in erythrocyte aggregation and adhesion].

It has been shown that rabbit red cells treated with formalin form aggregates in the presence of hyaluronic acid (HUA) soluble protein-chondroitin-keratan sulfate (PCKS) and cartilage proteoglycan aggregates (PA) but to a lesser degree than normal red cells. It is suggested that the proteoglycans under consideration can specifically interact with red cells. Aggregation of red cells in the presence of HUA, PCKS and PA is the result of the combined action of these two factors.