Compatibility Estimation of Oligobutadienediol with Simple Oligoetherpolyols for Molded Polyurethane Compositions Development
This article includes the results of compatibility of oligomeric hydroxyl-containing butadienerubber with oligoetherpolyols on the basis of propylene oxide (Laprols). The compatibility limits of liquid hydroxyl-containing butadiene rubber of Krasol LBH-3000V brand with polypropyleneglycols of Laprol brand with different molecular weights were determined.
Composites of Reduced Flammability Based on Amorphous Elastic Polyurethane and Halogen-containing Flame Retardant
The effect of a mixture of halogen-containing fl ame retardants based on chloroparaffins and 1,1,9-trihydroperfl uorononanol-1 immobilized on a montmorillonite carrier on the character of reducing the fl ammability of polyurethane was studied. Using X-ray diffraction and sol-gel analysis, the structural and morphological features of the elastomers obtained were studied. It has been revealed that intercalation of macromolecular chains of a matrix amorphous polymer into the intralayer spaces of a fl uorine-containing organoclay occurs with an increase in a degree of structural perfection of the macromolecular system that contributes to an increase in the fire resistance of the resulting polyurethane composites.
Molecular diversity of skin mucus lectins in fish.
Among lectins in the skin mucus of fish, primary structures of four different types of lectin have been determined. Congerin from the conger eel Conger myriaster and AJL-1 from the Japanese eel Anguilla japonica were identified as galectin, characterized by its specific binding to beta-galactoside. Eel has additionally a unique lectin, AJL-2, which has a highly conserved sequence of C-type lectins but displays Ca(2+)-independent activity. This is rational because the lectin exerts its function on the cutaneous surface, which is exposed to a Ca(2+) scarce environment when the eel is in fresh water. The third type lectin is pufflectin, a mannose specific lectin in the skin mucus of pufferfish Takifugu rubripes. This lectin showed no sequence similarity with any known animal lectins but, surprisingly, shares sequence homology with mannose-binding lectins of monocotyledonous plants. The fourth lectin was found in the ponyfish Leiognathus nuchalis and exhibits homology with rhamnose-binding lectins known in eggs of some fish species. These lectins, except ponyfish lectin, showed agglutination of certain bacteria. In addition, pufflectin was found to bind to a parasitic trematode, Heterobothrium okamotoi. Taken together, these results demonstrate that skin mucus lectins in fish have wide molecular diversity.