Biomedical subjects
S M Bychkov
Publications and source records attributed to S M Bychkov.
[Function of carboxyl and sulfate groups in proteoglycans].
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[The role of protein components of proteoglycans in steric exclusion of cells].
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[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 0.15 M NaCl solution. It was shown that both proteoglycans in the blood stream the aggregation action on the erythrocytes in the blood stream. The action finished after 24 hours later on the injection of proteoglycans during in which time the circulating the proteoglycans is remove out of the plasma.
[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. In pregnancy, the concentration of proteoglycans in the blood was constant at a low level throughout the period of pregnancy.
[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. It was shown that the rate of steric exclusion of erythrocytes depends on relationship between amount of erythrocytes and concentrations of these proteoglycans.
[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.
[Effects of various proteins on erythrocyte aggregation effected by proteoglycans].
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[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.
[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.
[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.
[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.
[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.
[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 (0.3-5.0 mg X ml-1) and HP-4 (0.3-5.0 mg X ml-1) was inhibited the aggregating action on the erythrocytes of HUP. Fraction HP-3 (0.3-5.0 mg X ml-1) was activated the aggregating action on the erythrocytes of PCHKSP. Fraction HP-4 when the concentration of their biopolymer were 0.3 mg X ml-1 so activated the aggregating action of PCHKSP, but when the concentration HP-4 0.6-5.0 mg X ml-1 was inhibited the aggregating action PCHKSP. The mixture of HP-3 (1.2 mg X ml-1) and HP-4 (1.2 mg X ml-1) was not influenced on aggregating action of PCHKSP.
[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.
[Analysis of the salts of cartilage proteoglycan aggregates].
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[Study of different proteoglycan salts].
The authors have devised the methods for preparing free hyaluronic acid (HA) and non-aggregating fraction of protein-chondroitin-keratan sulfate (PCKS), as well as those for preparing their Na+, K+, Ca2+ and Mg2+ salts (acid and neutral). Infrared spectroscopy has demonstrated the presence of intermolecular hydrogen bonds, formed by hydroxyl groups, in HA and PCKS macrocomplexes and in PCKS acid salts. HA salts appeared not to form macrocomplexes at the expense of intermolecular hydrogen bonds.