[A comparative study of carboxylesterase in the white mouse and in the caterpillar of the cotton bollworm Heliothes armigera]. / Sravnitel'noe issledovanie karboksilésterazy beloi myshi i gusenitsy khlopkovoi sovki Heliothis armigera.

Studies have been made on enzymic hydrolysis of p-nitrophenylacetate (p-NPhAc), n-nitrophenylbutyrate (p-NPhBu) and indophenylacetate (IPhAc) by carboxylesterase (CE) from mouse blood plasma and liver as well as from caterpillar of the cotton worm haemolymph, intestine and fat body. Different KM and V max values were obtained for CE from these sources. The highest specific activity of CE from mouse liver and caterpillar intestine and fat body was observed with p-NPhBu. p-NPhAc is the best substrate for CE from mouse blood serum and caterpillar haemolymph. Carboxylesterases from mouse and caterpillar differed in their sensitivity to armine and paraoxone by 1-2 orders depending on the substrate used. Species and tissue differences in the kinetics of CE-catalyzed reactions with different substrates and inhibitors were revealed.

Interferon system in patients with rheumatoid arthritis and sclerodermia systematica.

In the blood of patients with rheumatoid arthritis and/or sclerodermia systematica usually acid-labile interferon-alpha (IFN-alpha) was found. Blood leukocytes cannot be considered the source of its production as they spontaneously produce IFN-gamma identified with specific antiserum. Blood leukocytes of tested patients generated in vitro a reduced amount of staphylococcus enterotoxin A-induced IFN-gamma and virus-induced acid-labile IFN-alpha. This findings support the assumption of impaired functioning of T- and B-blood cells in autoimmune diseases. The production of Newcastle diseases virus-induced IFN-alpha and influenza virus-induced acid-stable IFN-alpha by patients' leukocytes has not been altered. Acid-labile IFN-alpha obtained from the blood of tested patients, IFN-gamma spontaneously generated by leukocytes in vitro and acid-labile IFN-alpha produced by leukocytes in vitro following induction with influenza virus show similar sensitivity to pH 2.0 and time patterns of the antiviral state development in human diploid fibroblast culture.

Production of alpha-interferon by human leukocytes.

We examined the capacity of human leukocytes to produce alpha-interferon subtypes following viral induction. It was shown that the beta-propiolactone inactivated viral inductor stimulated the production of a complete set of native alpha-interferon subtypes. Acid treatment of native interferon at pH 2.0 inactivated the acid-labile portion of alpha-interferon. Its exposure to 37 degrees C for 5 days and repeated acid treatment at pH 2.0 resulted in additional inactivation of some interferon pool fractions. The acid-labile subtypes of human alpha-interferon were formed in a nonadherent mononuclear cell fraction.

[Producer cells of human alpha and gamma interferons]. / Kletki--produtsenty al'fa- i gamma-interferonov cheloveka.

The cells responsible for production of human alpha and gamma interferons with proper inducers were studied using methods for fractionation of human blood mononuclear cells. The results indicated cooperation and mutual regulation by cells of interferon production. Monocytes were shown to play the leading role in the synthesis of acid-stable alpha interferon, whereas accessory cells were required for gamma interferon synthesis by T lymphocytes. Acid-labile alpha interferon was produced predominantly by B cells with accessory participation of T lymphocytes.

[Interferons produced by human leukocytes after induction with influenza virus]. / Interferony, vyrabatyvaemye leikotsitami cheloveka posle induktsii virusom grippa.

Influenza virus induces in human leukocytes the production of 3 types of interferon: 1--acid-labile, produced up to 3 days; 2--acid-stable, produced for 24 hours; 3--acid-stable, produced up to 3 days and showing antiviral activity in heterologous culture of cow embryo lungs alone. The heterogeneity of properties of the 3 interferon types appears to reflect heterogeneity of molecular weights of its components.