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M V Ostrovskaia

Publications and source records attributed to M V Ostrovskaia.

8 recordsLinked to original sources
PubMed1986

[Interaction of muscle glycogen phosphorylase B with F-actin].

The binding of rabbit muscle glycogen phosphorylase b to F-actin has been studied by sedimentation in analytical centrifuge in 10 mM Tris-acetate buffer pH 6.8 at 20 degrees C. The adsorption capacity of F-actin is equal to (7.8 +/- 0.9) X 10(-7) mole of glycogen phosphorylase b per 1 g of F-actin; the microscopic dissociation constant for the glycogen phosphorylase-F-actin complex is (5.4 +/- 0.5) X 10(-7) M. It was found that the allosteric activator, AMP, facilitates the adsorption of glycogen phosphorylase b on F-actin, whereas the substrate, Pi, and the inhibitor, ATP, cause an opposite effect.

Actins↗
PubMedDate not supplied

[Comparative study of the structure and protein composition of spermatozoid centrioles from sturgeons and salmon].

The aim of the present work was to compare the structure and protein composition of centrioles from spermatozoa of sturgeon and salmon fishes. The total protein content of the extracted fractions was studied by Na-SDS electrophoresis. Proteins with molecular weights from 15 to 170 kDa were detected. In both cases the major protein of centrioles is a protein with a molecular weight equal to that of tubulin. A protein with the molecular weight corresponding to actin was also detected. In both cases the ATPase activity stimulated by Ca2+ and Mg2+ ions was revealed. Electron microscopic studies showed differences in the ultrastructure of centrioles from sturgeon and salmon spermatozoa.

Adenosine Triphosphatases↗
PubMedDate not supplied

[Regulation of enzyme activity in adsorptive enzyme systems. III. Interaction of pig muscle lactate dehydrogenase with F-actin].

The binding of pig skeletal muscle lactate dehydrogenase by F-actin has been studied using the sedimentation method in 10 mM Tris-acetate buffer, pH 6.0 at 20 degrees C. Adsorption capacity of F-actin is equal to (1 +/- 0.1) . 10(-5) moles of lactate dehydrogenase per 1 g of actin. NADH decreases the affinity of F-actin with respect to lactate dehydrogenase. The binding of lactate dehydrogenase by F-actin in diminishing the rate of enzymatic reduction of alpha-ketoglutarate. The microscopic dissociation constant for the complex of the enzyme with F-actin which is estimated from the dependence of the enzymatic reaction rate of F-actin concentration at saturating NADH concentrations is equal (3.0 +2- 0.5) . 10(-7) M. It has been shown that the bound enzyme is characterized by the greater value of Km and the lower value of Vmax in comparison to the free enzyme.

Actins↗