(C) 2010 Elsevier Inc. All rights reserved.”
“Using tolylene-2,4-diisocyanate
as standard compound, the relationship between -NCO absorbance and concentration was studied with in situ FTIR. The linear relationship appeared correct only for concentrations lower than 0.4 mol L(-1). https://www.selleckchem.com/products/sb273005.html Then, the urethane reaction kinetics of phenol with tolylene-2,4-diisocyanate were investigated in different solvents, such as dimethyl sulfoxide, cyclohexanone, n-butyl acetate, 1,4-dioxane, and xylene. It showed that solvents largely affected reaction rates. The reaction was largely accelerated in polar solvents, following the order of dimethyl sulfoxide > cyclohexanone > n-butyl acetate > 1,4-dioxane > xylene. It was in contrast to the alcohol-diisocyanate reaction. Finally, an appropriate reaction mechanism was proposed. The H-O bond Fludarabine in phenol was polarized under the influence of solvents, which made the combination of hydrogen to nitrogen and alkoxyl group to carbenium easier. After that the solvent was dissociated and the carbamate generated. The kinetic equation could be derived as v = k’K center dot[S:] [ROH]center dot[R'NCO]. (C) 2011 Wiley Periodicals, Inc. J Appl Polym Sci 123: 580-584, 2012″
“PROTON GRADIENT REGULATION 3 (PGR3) contains 27
pentatricopeptide repeat (PPR) motifs and belongs to the P-subfamily. Previous studies have suggested that PGR3 functions in the stabilization of petL operon RNA and also in the translation of petL and one, or some, of the 11 plastid ndh genes encoding subunits of chloroplast NADH dehydrogenase-like complex (NDH). The pgr3-3 allele has been suggested to be specifically defective in the
putative PGR3 function of translation. Herein, we show that the polysome association of the monocistronic petL transcript is impaired in pgr3-3. We detected sequences weakly conserved Vorinostat manufacturer in the 5′ untranslated regions (UTRs) of petL and ndhA, and these putative elements were recognized by recombinant PGR3 in vitro. Previously, pgr3-2 was shown to be specifically defective in stabilizing petL operon RNA and to accumulate NDH at wild-type levels. Consistent with this pgr3-2 phenotype, we show here that a recombinant protein carrying the pgr3-2 mutation in the 12th PPR motif bound to the 5′ UTR of ndhA but not of petL. This indicates that a single amino acid alteration changes the binding specificity of PGR3. In contrast, the recombinant protein carrying the pgr3-3 mutation in the final, 27th, incomplete PPR motif can bind to both petL and ndhA 5′ UTRs, suggesting that the C-terminal end of PGR3 is not required for binding to targets but is essential for translation of petL and probably also ndhA. Our results fully support the model in which PGR3 recognizes two target sequences and is involved in multiple functions, i.e. stabilizing RNA and activating translation.