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Biomedical subjects

L K Shataeva

Publications and source records attributed to L K Shataeva.

At least 19 recordsLinked to original sources
PubMed1975

Some properties of the protease from Aspergillus terricola.

The protease from Aspergillus terricola (terrilytin) was isolated and purified by the ion exchange method and by gel chromatography. The data on its molecular weight, isoelectric point, N-terminal amino acids were described. The protease included polysaccharide which stabilized the enzyme activity under the storage and lyophylization. Polysaccharides isolated from different fungi and yeasts were found to stabilize and activate terrilytin rising the affinity of enzyme to substrate. Terrilytin was revealed to exhibit the thrombolytic effect and expressive affinity to the fibrin in comparison with other substrates of high and low molecular weight. The enzyme showed the antigenic activity. From immune rabbit sera 7S gamma-globulins inhibiting proteolysis of caseine and 19S gamma-globulins activating the proteolysis of fibrin and fibrinogen by terrilytin were isolated by gel chromatography.

Amylases↗
PubMedDate not supplied

[Preparative isolation of gonadotropin and urokinase on carboxylic cation exchangers].

Low-pressure ion-exchange chromatography was used for sequential isolation of chorionic gonadotropin and urokinase (EC 3.4.99.26) from urine of pregnant women. Theoretical analysis of electrostatic interactions of protein macromolecules with the sorptive surface of a carboxylic cation exchanger was performed. This analysis allowed us to optimize the pH values for selective sorption and reversible desorption of the target component on a cation exchanger with a selected acidity of functional groups. The use of carboxylic cation exchangers KM-2p and Biokarb-GM allowed us to obtain the preparations with purity not inferior to commercially available preparations.

Animals↗
PubMedDate not supplied

[Tissue-specific nucleoprotein complexes].

A method of isolation of native nucleorprotein complexes from cattle cerebral cortex, thymus, and liver was developed. Compositions of these complexes were studied by means of gel-chromatography and ion-exchange chromatography. These preparations were shown to consist of several fractions of proteins and their complexes differ by molecular mass and electro-chemical properties. Native nucleoprotein complexes revealed high tissue specific activity, which was not species-specific.

Animals↗
PubMedDate not supplied

[Nucleoprotein complexes of yeast and their biological effect on T-lymphocytes].

Complexes of nucleic acids and acid nuclear proteins that are active toward human T-lymphocytes were isolated from cells of bakers' yeast Saccharomyces cerevisiae. The conditions of isolation of nucleoprotein complexes by acid extraction followed by microfiltration for concentration of macromolecular components were optimized. Gel filtration and electrophoresis were used to study the composition and molecular weights of components of the preparations obtained. It was shown that nucleoprotein complex had a molecular weight of 1430 kDa. However, only one zone was determined by electrophoresis of the protein component with a molecular weight of 30 kDa.

Fungal Proteins↗
PubMedDate not supplied

[Affinity chromatography of nucleoprotein complexes].

Affinity sorbent containing cellular membranes of the cerebral cortex was obtained by means of an inclusion into porous matrix of polyacrylonitrile. Sorption of model and natural nucleoprotein complexes on the obtained sorbent was studied by the method of affinity chromatography. Distribution coefficients were determined. Natural nucleoprotein complexes isolated from brain possess a greater selectivity of binding to the cellular membranes of the cerebral cortex than that from liver.

Acrylic Resins↗
PubMedDate not supplied

[On the effect of immune and normal sera on catalase].

Effect of specific immune and normal sera on catalase was studied. The sera activated the enzyme, partially protected catalase against UV-irradiation and heating and also against the effect of inhibitors. Antibodies against catalase were observed in the fraction of 7 S gamma-globulins of immune serum. In studies of heat denaturation of catalase the stabilizing effect of immune serum was more distinct than the influence of normal serum and its protein fractions. In presence of serum protein fractions there was a correlation between the enthalpy of heat denaturation of catalase and decrease in specificity of the protein, in respect to the enxyme, associated with it in a complex. Alterations in enthropy compensated completely the decrease in enthalpy.

Animals↗
PubMedDate not supplied

[Effect of normal and specific immune sera on neuraminidase activity].

We have got evidence that there is no antigenic relationship reflecting the structural similarity between neuraminidases synthesized by noncholera vibrios and Arthrobacter nicotianae. The cross-reactions between the enzymes and heterological antisera were not observed. Antibodies against the A. nicotianae neuraminidase inhibited the activity of the enzyme for a glycomacropeptide of milk whey and for components of the blood serum, and had no effect no the neuraminidase from noncholera vibrios. Antibodies against the neuraminidase of noncholera vibrios inhibited only the activity of the homologous enzyme. Upon gel-filtration on Sephadex G-200 the antibodies inhibiting the activity of the enzymes under study were found in the fraction of 7S-gamma-globulins.

Animals↗
PubMedDate not supplied

[The use of a glycomacropeptide of kappa-casein as a substrate for neuraminidase].

Glycomacropeptide from milk was studied; its molecular mass and amino acid composition were evaluated. When the glycomacropeptide was used as a substrate of neuraminidase, it exhibited many advantages as compared with ovomucin (high molecular substrate of the enzyme) due to increased content of sialic acids in the glycomacropeptide composition and to high solubility.

Amino Acids↗
PubMedDate not supplied

[Structure and sorption properties of regenerated hemosorbent SCN].

Stepwise desorption of protein components from the hemosorbent SCN after hemoperfusion was studied, and their molecular weights were determined. It was found that hard alkaline regeneration and oxidation with nitric acid do not affect the hemosorbent structure, composition and potentiometric characteristics. The regenerated hemosorbent can be successfully used for adsorbtion of extraneous low- and medium-molecular weight components to clarify microbiological liquids.

Adsorption↗