[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.

[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.

[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.

Isolation and study of the properties of an interferon-like inhibitor of viruses from normal human blood serum.

A protein with a molecular weight of 17,400 daltons and an isoelectric point at pH 4.9 has been isolated from the blood serum of healthy donors by successive ion-exchange chromatography of QAE-Sephadex A-50, affinity chromatography on DNA-cellulose, and polyacrylamide gel electrophoresis, in the presence of sodium dodecyl sulfate. The protein isolated, like interferon, suppresses the development of the cytopathogenic action of the viruses of vesicular stomatitis and murine ecephalomyocarditis in cultures of human cells of the L-41 and M-19 lines.

[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.

[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.

[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.

[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.

[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.