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Biomedical subjects

B F Sukhomlinov

Publications and source records attributed to B F Sukhomlinov.

At least 19 recordsLinked to original sources
PubMed1991

[A method of fractionating bone marrow cells in a density gradient using a mixture of Ficoll and Verografin].

The authors suggest a method for hemopoietic tissue cell fractionation into populations enriched for various hemopoietic elements. Centrifugation in a three-layer density gradient of mixtures of ficoll and verografin (d1 = 1.03 g/cm3, d2 = 1.09 g/cm3, d3 = 1.1 g/cm3) resulted in three fractions. The first contained lymphoid cells, the second erythroid cells (89.1 +/- 7.3%), and the third consisted of white blood cells (78.5 +/- 6.3%).

Animals↗
PubMed1989

[Amino acid sequence of Ondatra myoglobin (Ondatra zibethica). Characteristic features of myoglobins from semiaquatic animals].

Based on the amino acid composition of globin, amino acid analysis and N-terminal sequencing of peptides as well as a comparative analysis of the primary structure of beaver, coypu rat and otter myoglobins with the use of the fingerprinting technique, the amino acid sequence of the major component of ondatra myoglobin including 153 amino acid residues was reconstructed. The results of a comparative analysis of the primary structure of myoglobin and the peculiarities of the functional morphology of myoglobins from semi-aquatic animals and sperm whale and the role of amino acid substitutions in the spatial structure of ondatra myoglobin are discussed.

Amino Acid Sequence↗
PubMed1987

[Cationic blood proteins in suppurative and septic processes].

The level of cationic proteins was studied in 52 patients with peritonitis and purulent processes of soft tissues. The authors have shown its elevation to be dependent on the degree of the disease. The improved state of the patients and recovery was followed by a decreased content of cationic proteins in blood, their fractional composition being normalized.

Blood Proteins↗
PubMedDate not supplied

[Comparative study in structure of myoglobins in semiaquatic animals: Castor fiber, Ondatra Zibethica, Lutra lutra].

A degree of similarity in the structure of myoglobins in the semiaquatic animals (beaver, muskrat, otter) is shown by the finger-print method with the determination of amino acids content in peptides. It is established that about 2/3 of the acid sequence in the investigated myoglobins are invariable. An assumption is advanced that these regions of the structure are of most importance in the functional respect.

Amino Acid Sequence↗
PubMedDate not supplied

[The effect of hypoxic hypoxia on the activity of glycolysis enzymes in rat erythrocytes].

The oxygen-binding properties of hemoglobin, concentration of 2,3-diphosphoglycerate, activity of carbohydrate metabolism enzymes and kinetics of rat erythrocyte hemolysis have been studied at high altitudes. The hemoglobin affinity to oxygen, glycolysis enzyme activity and erythrocyte membrane resistance are established to increase at the initial period of adaptation. The activation of the pentose-phosphate pathway of the glucose, transformation and inhibition of the glycolytic process in these cells are observed on the 10th day.

2,3-Diphosphoglycerate↗