[Antiviral activity of derivatives of aldehydophenols, aldehydo- naphthols and sugar derivatives]. / Protivovirusnaia aktivnost' proizvodnykh al'degidofenolov, al'degidonaftolov i proizvodnykh sakharov.

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.

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. The amino acid composition of the protein isolated differs from those of various fractions of human interferons.

[DNA-binding proteins in human serum]. / DNK-sviazyvaiushchie belki syvorotki krovi cheloveka.

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.