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Kh A Aslanov

Publications and source records attributed to Kh A Aslanov.

10 recordsLinked to original sources
PubMed1992

[Interferon-inducing activity of hydroxybenzylamine derivative].

Interferon-inducing activity of the interferon inductor savrats, an oxybenzylamine derivative of was studied. It was shown on experimental animals that along with its low toxicity, savrats had a high interferon inducing capacity. There were early and late peaks of interferon production (4-8 and 48-96 hours later, respectively) depending on the route of the inductor administration. It was noted that for optimization of the schemes for using interferon inductors, careful choosing of the drug pairs participating in the induction and employment of various routes for administration of the same drug are required.

Administration, Oral↗
PubMed1991

[Relation between interferon-inducing activity of natural interferon inducers and their chemical structure].

The interferon-inducing activity of new derivatives of gossypol, a low molecular weight natural polyphenol, and its model compounds was studied in regard to their chemical structure. The active groups required for development of optimal interferon inductors on the basis of the natural polyphenols were defined. As a result of the studies the new interferon inductor AC-1 which is a condensation product of gossypol, a natural polyphenol, and a cellulose derivative was isolated. The interferon-inducing activity of AC-1 was investigated with respect to its dose and the administration route. High interferon-inducing activity of the interferon inductor after its administration by any route in doses of 10 to 100 mg/kg was demonstrated. The serum interferon titers reached 2560 units/ml.

Administration, Oral↗
PubMed1982

[Biosynthesis and post-translational maturation of transferrin in subcellular fractions of rat liver].

Using [14C]leucine pulse label in vivo, the dynamics of transferrin synthesis and its intracellular transport in rat liver and the changes in the molecular sizes of the newly formed transferrin chains during this transport were investigated. The transferrin radioactivity peaks in the rough and smooth endoplasmic reticulum and in Golgi vesicles were observed on the 15th, 20th and 20-30th min after injection of the pulse label. In blood stream the [14C]transferrin was detected 30 min after the label administration, the maximum of radioactivity being observed on the 60th min. The intracellular transport of transferrin was accompanied by changes in its molecular weight. The molecular weights of the transferrin precursors from the rough and smooth endoplasmic reticulum, of immunoreactive transferrin from Golgi vesicles and of circulating transferrin are 86 000-88 000, 84 000 and 77 000, respectively. These variations in molecular weights are indicative of a complex reaction sequence of posttranslational maturation of transferrin in the liver, which includes in all probability proteolysis and glycosylation.

Animals↗
PubMed1981

[Properties of rat liver polyribosomes synthesizing transferrin].

A radioimmunological study of rat liver polyribosomes synthesizing transferrin was carried out. The 125I-labelled monospecific antibodies against transferrin interact with membrane-bound liver polyribosomes to form a specific antigen-antibody complex. No binding of 125I-antibodies against transferrin to free liver polyribosomes was observed. The transferrin polyribosomes contain 11-13 monoribosomes per 1 molecule of mRNA. An injection of cycloheximide to the animals results in an increase in the size of the transferrin polyribosomes up to 16 monoribosomes per 1 mRNA molecule. During translation of the liver polyribosomal fractions in a cell-free system of wheat embryos only the membrane-bound polyribosomes were capable to synthesize immunoprecipitated transferrin.

Animals↗
PubMed1978

[Ephedrine, salsoline and cytisine derivatives as substrates and inhibitirs of cholinesterases].

25 iodomethylates of acetic, propionic, butyric, isobutyric and valeric esters of N-(beta-hydroxyethyl)-derivatives of ephedrine (I) pseudo-ephedrine (II), salsoline (III), salsolidine (IV) and cytisine (V) are studied as substrates and inhibitors of acetylcholine esterase (EC 3.1.1.8) from human erythrocytes and butyrylcholine esterase (EC 3.1.1.8) from horse serum. Butyrylcholine esterase found to increase the hydrolysis rate of all the alkaloid esters studied with the increase of acyl radical either to valerates (for ephedrine and pseudo-ephedrine derivatives), or to butyrates (for the rest alkaloids) and then it did not considerably change under further elongation of carbon chain up to valerate. Isobutyrates were observed to be similar to propionates in their hydrolysis rates. Acetylcholine esterase hydrolyzed acetates with the highest rate, while butyrates of ephedrine and pseudoephedrine derivatives were hydrolyzed by the enzyme 2,5-3-fold as slow as acetates. The rate of choline esterase hydrolysis decreased in the row: ephedrine--salsoline--cytisine with the volumetric increase of the cationic group. The decrease was almost 10-fold for butyrylcholine esterase, while a transition from "poor" substrates to reversible inhibitors was observed for acetylcholine esterase (3 of 5 cytisine esters were reversible inhibitors of the enzyme). The data obtained are compared with literary data on other cyclic choline esterase substrates; they are discussed from the viewpoint of unproductive binding hypothesis and on the basis of the structure of active centres of acetyl- and butyrylcholine esterases.

Acetates↗
PubMedDate not supplied

[Antiviral activity of derivatives of aldehydophenols, aldehydo- naphthols and sugar derivatives].

The antiviral activity of aldehydrophenol, aldehydonaphthol derivatives and sugar derivatives was studied. The compounds in doses of 150-500 micrograms/ml were shown to reduce the viral infectious activity by 1.5-3.3 lg TCD50/ml. The degree of virus activity inhibition by the synthesized compounds indicates the relationship of the chemical structure with the antiviral effect of these compounds.

Animals↗
PubMedDate not supplied

[Binding of gamma-aminobutyric acid in the synaptic membranes of rat brain].

The Na+-dependent and Na+-independent (receptor) binding of [3H] GABA is measured in rat brain synaptic membranes. The receptor binding is presented by at least 3 types of binding sites differing in kinetic parameters (dissociation constants and maximal concentration of binding sites). Phenyl-GABA and pyracetam do not affect receptor binding while 4-hydroxybutyric acid, apamine and bicuculline inhibit it with inhibition constants K1=100, 2 and 1 micron, respectively. Solubilization of synaptic membranes with 2% potassium cholate in the presence of total brain phospholipids does not inactivate [3H] GABA receptor binding.

Animals↗
PubMedDate not supplied

[DNA-binding proteins in human serum].

Fractions of acid and base blood serum proteins, separated by ion exchange chromatography on QAE-Sephadex (but not the proteins of the whole blood serum, which had the same charge), reacted with DNA preparations. Separate fractions of blood serum proteins were able to react with DNA after electrophoretic separation. Binding of blood serum proteins with DNA did not depend on ion strength within the range of NaCl concentration from 0.1 M to 0.5 M; it was also stable at pH 5.5 = 8.0. Interaction between acid DNA-binding proteins and native DNA was inhibited by denatured DNA, polyguanilic and polyinosinic acids and by other polyanions: dextran sulfate, polyvinyl sulfate, polyanetol sulphonate, polystyrol sulphonate and heparin. Acid DNA-binding proteins showed only a slight affinity to polyadenilic, polyuridilic and polycytidilic acids. The acid and base DNA-binding proteins appear to be contained in blood serum in the form of a loosely bound complex.

Blood Proteins↗