Changes in the amino acid sequence of hemagglutinin during sequential adaptation of human influenza virus A to replication in mice

The primary structure of hemagglutinin (HA) gene of Influenza virus A/USSR/90/77 (H1N1) variants after 3 and 11 passages has been determined. In the HA1 coding region of mice-adapted virus (11 passages) there are two amino acid substitutions: Thr 89----Ala and Asn 127----Asp. At the first stage of adaptation (3-rd passage) only a single mutation was detected: Asn 127----Asp. The adaptation is accompanied by the loss of specific carbohydrate attachment sites adjacent to the receptor-binding site located at HA1 subunit with a concomitant variation in antigenicity.     

Actin participates in the structure of liver intermediate filaments

A dominating protein fraction (p45) having molecular weight of 45000 and pI 5.45 was found in the intermediate filaments pellet obtained from rat liver besides the present cytokeratins. Peptide mapping and radioimmunological assays with antibodies against this protein and muscle actin proved that the p45 protein belongs to the actin group. Immunoelectron microscopy revealed that this protein is located on the liver intermediate filaments. By melting of the cytokeratin complexes in urea it was established that p45 protein is complexed with the low molecular weight cytokeratin.     

Behavior of a dust grain in the double layer of an electric probe in a gas-discharge plasma

Equations for the motion of an individual dust grain in the double layer of a negatively charged cylindrical probe in a glow discharge plasma are derived and solved numerically. The distribution of the electric potential near the probe is determined, and the grain charge is calculated as a function of the distance from the probe for different probe potentials. The trajectories of grains with different initial energies are traced. An analysis of the grain trajectories shows that, at a certain distance from the probe, high-energy grains may be recharged; i.e., the grain charge may change sign. The grains are found to have no direct effect on the probe current in a dusty plasma of a glow discharge.     

Features of peroxidase oxidation of amidopyrine and its analogs]

Peroxidatic oxidation of N-alkyl and sulfalkyl-substituted 4-aminopyrazolones (amidopyrine and metapyrine) is mediated by oxyperoxidase, whereas the oxidation of non-substituted 4-aminoantipyrine occurs via the classical peroxidase cycle, without oxyperoxidase accumulation. The free radicals formed at the first step of the oxidation cycle show a tendency for disproportionation and exchange. During catalysis in heavy water the oxidation of substituted aminopyrazolones is accelerated by plant peroxidase. This effect is due to the activation of the second oxidative state of the enzyme. Complete peroxidatic oxidation of amidopyrine results in the formation of several reaction products. The main product is not identified as dioxypyramidone formed via nonenzymatic peroxidatic oxidation. The oxidation of the indicator (azopyram) which represents an amidopyrine-aniline mixture results first in the formation of amidopyrine radicals. The reaction product (dye) is formed via the binding of these radicals to aniline radicals. The latter are predominantly formed via a nonenzymatic route during the reduction of the amidopyrine radicals by aniline. Similar to the formation of azopyram and the full oxidation of amidopyrine, this reaction is accompanied by the displacement of the substituents from the 4-amino group.