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Biomedical subjects

I A Chernova

Publications and source records attributed to I A Chernova.

10 recordsLinked to original sources
PubMed1981

[Method of applying colchicine to the rat vagus nerve for the purpose of selective action on axonal transport].

A method of local application of colchicine deposited in a wax and paraffin alloy to the nerve is suggested. The doses of 25, 50, 75 and 100 micrograms were tested. Four days after application of 75 and 100 micrograms of colchicine, light microscopy demonstrated a non-uniform thickening of neurofibrils and the increase in their argyrophilic properties. Electron microscopy discovered the reduced number of microtubules, disordered arrangement of neurofilaments and accumulation of the latter ones beneath the neurolemma. The overall electric activity of the nerve was not disturbed. The method of colchicine application in vivo ensures the prolonged action of the drug without nerve compression or injury, thereby enabling one to assess consistently the sequels of the blockade of neurotrophic factors for metabolism of the innervated structures.

Animals↗
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

[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

[Blood group-specific variability of sialic acid contents in the chorionic gonadotrophin structure].

Low-pressure ion-exchange chromatography was used for isolation of chorionic gonadotropin (hCG) from urine of pregnant women. The purified hCG-preparations from various blood group donors were shown to differ in their sialic acid content. The highly purified hCG-preparations after gel chromatography were analyzed in the reaction of hemagglutination and the preliminary results suggest their blood group specificity.

Adult↗
PubMedDate not supplied

[Measuring neuraminidase activity by the thiobarbiturate method].

A number of reducing agents used for removing the excess of periodate in the reaction of the neuraminidase (EC 3.2.1.18) activity measuring by the thiobarbituric acid technique were compared. The toxic reagent sodium arsenite may be replaced by a 20% solution of ascorbic acid. The modified technique of the neuraminidase activity determining can be used in case of both high-molecular weight substrate ovomucin and low-molecular weight substrate-glycomacropeptide from milk whey.

Indicators and Reagents↗
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↗