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Biomedical subjects

I M Bystrova

Publications and source records attributed to I M Bystrova.

12 recordsLinked to original sources
PubMed1991

[Study of chemically modified hemoglobin as an artificial oxygen carrier in the model of hemorrhagic shock in dogs].

Hemodynamic and gas-transporting properties of the chemically modified hemoglobin solution have been studied on the model of hemorrhagic shock in dog. It has been shown that the polymerized hemoglobin solution exerts the hemodynamic action just as the plasma substitute "polyglucin" does. However, in contrast to the latter, polyhemoglobin circulating in the vascular bed for a prolonged period of time increases the blood oxygen capacity and oxygen delivery to tissues with the resultant increase in body total oxygen taking-up.

Animals↗
PubMed1989

[Changes in the peripheral blood, liver and spleen during the long-term experimental administration of modified hemoglobin].

The study of chronic toxicity of polymerized hemoglobin solutions (PHb) has demonstrated the relationship between the dose of the solution administered and the level of functional and morphological changes induced in various organs of experimental animals. Lower doses (1.8 g/kg) of PHb had no effect on the values of protein and carbohydrate metabolism, while the high doses (10-15 g/kg) of PHb resulted in the impairment of protein synthesis, morphological changes in the spleen and lymphatic nodes.

Animals↗
PubMedDate not supplied

[Study of oligohemoglobin solutions in vitro and in vivo].

Solutions of oligohemoglobins (OHb) with middle molecular mass 100 x 10(3) = 400 x 10(3), obtained after polycondensation of hemoglobin with glutaric aldehyde as well as oligohemoglobin modified with pyridoxal-5-phosphate, were studied in vivo and in vitro (plethoric administration, isovolemic metabolic substitution, hemorrhagic shock; at a dose of 0.5-1.8 g/kg of body mass; dogs, rabbits, rats). With increase of the OHb molecular mass period of its circulation in blood was elevated; blood plasma protected OHb from autooxidation; half-life of OHb was about 12-18 hrs in isovolemic metabolic substitution and in hemorrhagic shock and about 5 hrs--in plethoric administration. During circulation molecular mass selection of OHb occurred, where low molecular fraction decreased and high molecular fraction--accumulated; sign and value of human erythrocyte charge were similar both in OHb solutions with concentration up to 5% and in physiological solution.

Animals↗
PubMedDate not supplied

[Testing the activity of enzymes responsible for biosynthesis of purine nucleotides AIR-carboxylase and SAICAR-synthetase in human cell extracts].

Activities of AIR-carboxylase (ES 4.1.1.21) and SAICAR-synthetase (EC 6.3.2.6) were found in lysates of human erythrocytes, thrombocytes and leukocytes and in homogenate of the stomach biopsy sample. However, these activities were absent in blood plasma and bile. The human erythrocyte enzyme preparation, which had both activities, was isolated and purified about 200 times. The copurification of both activities and properties of the enzyme preparation suggest that two consecutive reactions of purine biosynthesis de novo (from AIR to SAICAR) in human cells are catalyzed by one bifunctional enzyme which is probably encoded by one gene.

Carbon-Nitrogen Ligases↗
PubMedDate not supplied

[Composition and various properties of acetylcholinesterase from human erythrocytes].

Composition and some properties of human erythrocyte acetylcholinesterase prepared for use in medical practice were studied. After electrophoresis 5 protein bands, two of which exhibited the enzymatic activity, were detected in the preparation. Three isoenzyme forms of acetylcholinesterase, dissimilar in their electrophoretic mobility, were detected in the preparation by ion exchange chromatography on DEAE Sephadex A-50. The preparation did not contain hemoglobin, thromboplastic substances and group isoagglutinogens A and B.

ABO Blood-Group System↗
PubMedDate not supplied

[Chromatographic analysis of the hemin isolated from the erythocytes of hematological patients].

Fractional composition of hemin, isolated from blood of patients with hematological impairments, differed from the composition characteristic for donors as shown by paper chromatography. Three fractions of hemin, which corresponded to various steps of polymerization of the substance, were found on chromatograms of donor hemin. Hemin from the patients were characterized by alteration both in amount and in the ratio of the fractions. Estimation of the hemin composition using paper chromatography might serve as an additional diagnostic test.

Chromatography, Paper↗