Polymeric composite with high thermodynamic properties

The possibility of obtaining a thermostable film composite material based on a mixture of polyvinylidenefluoride and polyamidebenzimidazole with NTsS piezoelectic ceramics as a filler was studied. Its thermal characteristics were determined and compared with those of separate polymers.     

Preparation of derivatives of DL-estrone and of 19-norsteroids from 3-methoxy-Δ1,3,5,(10),9(11)-8,14-secoestratetraen-14,17-dione

Summary Starting from S-methoxy-^{1,3,5(10),8,14}-estrapentaen-17-one (II) and its ethylene ketal (III), a combination of hydrogenation, reduction by Birch's and Johnson's methods, and other reactions has given the methyl ethers of DL-estrone and DL-estradiol (I) and (XV), and also DL-19-nortestosterone (XVI), ^4,8-19-norandrostadienedione (VIII) and other steroids.     

Small-angle X-ray scattering study of the structure of self-organized polymer matrices and formation of imbedded metal nanoparticles

The structures of self-organizing polymer matrices based on collapsed gels and polyoctadecylsiloxanes have been studied by the methods of conventional and anomalous X-ray small-angle scattering with the use of the laboratory and synchrotron sources of X-ray radiation. The process of formation of metal nanoparticles in such matrices is also studied, their size distributions are calculated, and the models of localization of these particles in the polymer matrices are suggested. It is shown that growth of metal particles is controlled by the structure of the polymer network and is limited by the dimensions of its cells. The electron-density profiles of polycondensed octadecylsiloxane matrices are also calculated.     

Quantitative fast fractionation of a pool of polyclonal antibodies by immunoaffinity membrane chromatography.

A new affinity method for the direct quantitative analysis of monospecific anti-peptide immunoglobulins (antibodies) and, simultaneously, their semi-preparative isolation from blood serum of the immunized animals has been developed. Immunoaffinity discs based on macroporous poly(glycidyl methacrylate-co-ethylene dimethacrylate) were used as the supporting stationary phase. The specifically prepared synthetic peptides with biological activity imitating that of the immunoglobulin binding sites of various proteins were used as the selective ligands instead of native proteins. These ligands were immobilized by a single-step reaction that involves epoxy groups located on the pore surface of the porous polymer disc with amine groups of the peptide molecules. A spacer between biospecific ligands and the linking site was not required to achieve good separation. These novel immunosorbents characterized by large binding capacity are well suited for high throughput screening. Dissociation constants of the peptide-antibody complexes calculated from the experimental adsorption isotherms confirm the excellent selectivity of the proposed separation method. The discs were used in a single step enrichment of antibodies both from precipitated blood fraction and crude blood serum of immunized animals. The quantitative data of the immunoaffinity disc chromatography were compared to those obtained by an enzyme-linked immunosorbent assay. Gel electrophoresis was also used to demonstrate the high degree of purity of the final product. In contrast to typical techniques that involve proteins, this immunoaffinity approach allows for the first time direct determination of concentration of specific antibodies using the immunosorbent prepared from the short peptide molecules immobilized on the internal surface of reactive porous polymer discs.