Hydrogenation of the phosphatidylcholine of Helianthus annuus

Summary 1. The optimum conditions have been found for the exhaustive hydrogenation of chromatographically pure phosphatidylcholine of plant origin on a Pd/Al catalyst.2. It has been shown that under the conditions of the enzymatic hydrolysis of the hydrogenated phosphatidylcholine by kufi venom phospholipase A at pH 10.15 the specificity and activity of the enzyme are retained.3. The main physical and chemical indices of the hydrogenated phosphatidylcholine and of the products of its hydrolysis are given.Institute of the Chemistry of Plant Substances, Academy of Sciences of the Uzbek SSR, Tashkent. Translated from Khimiya Prirodnykh Soedinenii, No. 1, pp. 38–41, January–February, 1976.     

Reaction of yeast inorganic pyrophosphatase with inorganic phosphate labeled with radioactive phosphorus

Conclusions The reaction of yeast inorganic pyrophosphatase with inorganic [p³²]phosphate forms a phosphorylated enzyme.     

Synthesis of β-(4,5-dihalofuryl)acrylic and -propiolic acids

Reaction of 4,5-dihalofurfurals with acetaldehyde and with carbethoxybromomethylenephosphorane gave, respectively, 4,5-dihalofurylacroleins and -(4,5-dihalo-2-furyl)--bromoacrylic acid esters. The latter were converted to 4,5-dihalo-2-furylpropiolic acids by the action of alkali.Translated from Khimiya Geterotsiklicheskikh Soedinenii, No. 3, pp. 315–317, March, 1978.     

Novel π-conjugated structures with fluorescent properties based on 4-alkoxytetrahydroquinazoline N-oxide

Russian Chemical Bulletin - Synthetic approaches to previously unknown 4-OR-2-methyltetrahydroquinazoline N-oxides were elaborated. 4-Alkoxy- and 4-aryloxy-2-methyltetrahydroquinazoline N-oxides...     

Structural investigations of <Emphasis Type="Italic">E. Coli</Emphasis> dihydrolipoamide dehydrogenase in solution: Small-angle X-ray scattering and molecular docking

Dihydrolipoamide dehydrogenase from Escherichia coli (LpD) is a bacterial enzyme that is involved in the central metabolism and shared in common between the pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes. In the crystal structure, E. coli LpD is known to exist as a dimer. The present work is focused on analyzing the solution structure of LpD by small-angle X-ray scattering, molecular docking, and analytical ultracentrifugation. It was shown that in solution LpD exists as an equilibrium mixture of a dimer and a tetramer. The presence of oligomeric forms is determined by the multifunctionality of LpD in the cell, in particular, the required stoichiometry in the complexes.     

DNA interaction with synthetic polymers in solution

DNA complexes with cationic polymers (polyvinylamine (PVA), polyallylamine (PAA), polydimethylaminoethylmethacrylate (PDMAEM), poly-(N,N,N-trimethylammonio)ethyl methacrylate chloride (PTMAEM), poly-l-lysine (PLL)) were investigated. It was shown that volume and persistent length of DNA do not change essentially at low cationic polymer concentration in a solution. DNA packaging in 0.005 M NaCl was observed at charge ratio N/P ≈ 1. Secondary DNA structure in complexes was not disrupted, and DNA was protected from protonation. The comparison between DNA packaging in complexes with polycations and DNA condensation induced by trivalent ions was made.