Reaction of a silicon trialkoxide w i t h magnesium or nickel chloride leads to a n e w polymer in which organic side chains are linked t o a phyllosilicate-like framework through Si-C covalent bonds.
A light diffuser film based on hollow silica nanoparticles as fillers was facilely fabricated by coating suspension of the particles in a UV-curable acrylate monomer solution on a cleaned glass substrate. The amount of the particles in the films was varied from 5 to 20 vol%. The optical properties and the light diffusing ability of the films were then studied and further compared to those of the cleaned glass. The result revealed that the films become opaque when the amount of the particles increases. The increment of the particles also leads to the formation of aggregated particles with a larger size and homogeneous dispersion as the FE-SEM images had been presented. Although the films exhibit the opacity, their total transmittance is still high and close to the cleaned glass transmittance. Moreover, the improved diffuse transmittance of the films is obtained from the increased amount of the particles. The increment of the particles also provides the different scattered light image sizes with a homogeneous light resulting in a distinct light diffusing ability. Those results indicated that the films based on the hollow silica nanoparticles as fillers are probably applied for light diffuser films in the LCD industry.
Alanine dehydrogenase (AlaDH) was purified to homogeneity from cell-free extracts of a non-N2-fixing filamentous cyanobacterium, Phormidium lapideum. The molecular mass of the native enzyme was 240 kDa, and SDS-PAGE revealed a minimum molecular mass of 41 kDa, suggesting a six-subunit structure. The NH2 terminal amino acid residues of the purified AlaDH revealed marked similarity with that of other AlaDHs. The enzyme was highly specific for L-alanine and NAD+, but showed relatively low amino-acceptor specificity. The pH optimum was 8.4 for reductive amination of pyruvate and 9.2 for oxidative deamination of L-alanine. The Km values were 5.0 mM for L-alanine and 0.04 mM for NAD+, 0.33 mM for pyruvate, 60.6 mM for NH4+ (pH 8.7), and 0.02 mM for NADH. Various L-amino acids including alanine, serine, threonine, and aromatic amino acids, inhibited the aminating reaction. The enzyme was inactivated upon incubation with pyridoxal 5'-phosphate (PLP) followed by reduction with sodium borohydride. The copresence of NADH and pyruvate largely protected the enzyme against the inactivation by PLP.
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