The Arabidopsis homologue of an eIF3 complex subunit associates with the COP9 complex

The Arabidopsis COP9 complex is a multi-subunit repressor of photomorphogenesis which is conserved among multicellular organisms. Approximately 12 proteins copurify with the COP9 complex. Seven of these proteins are orthologues of subunits of the recently published mammalian COP9 complex. Four of the proteins show amino acid similarity to various subunits of the COP9 complex, eIF3 complex and 19S cap of the proteasome. We have studied one of these proteins in order to determine if it is a component of the COP9 complex. Arabidopsis p105 is highly similar to the p110 subunit of the human elF3. The p105 gene is induced during photomorphogenesis, and RNA and protein analysis reveal different tissue accumulation patterns. p105 is found in a large protein complex. p105 interacts in yeast with both COP9 and FUS6, two known components of the COP9 complex. Our results indicate that p105 is not a component of the COP9 core complex, though it may interact with components of the complex.     

Responses of maxillary sensilla styloconica inBombyx mori to glucosides fromOsmunda japonica,a nonhost plant

We isolated glucosides from the royal fern,Osmunda japonica, which elicit a deterrent response in larvae ofBombyx mori. These compounds were absent in taro (Colocasia antiquorum) and castor-oil plant (Ricinus communis) leaves and did not evoke responses of sensory cells in the lateral and medial sensilla styloconica ofSpodoptera litura. This glucoside extract of the royal fern leaves stimulates receptors generally associated with deterrent. It is also possible that this compound may act as a behavioral deterrent, and from actual feeding tests, it is suggested that this compound may prevent feeding in some monophagous insects, such asBombyx mori. The deterrent glucoside possesses a noncyclic aglycon.     

Expectancy theory prediction of the goal theory postulate, "The harder the goals, the higher the performance."

Goal theory postulates that harder goals lead to higher performance than do easier goals. The present study tested the prediction, based on expectancy valence theory, that this would be true only if the payoff for succeeding at the harder goal is sufficiently greater than the alternatives to compensate for its greater difficulty. 63 undergraduates were each given an easy and a hard task/goal, requiring the comparison of paired sets of 3-digit numbers. Expectancy theory measures for the 2 goals were obtained from Ss. Performance was higher for the hard goal than for the easy goal, supporting the goal theory postulate. Force was also higher for the hard goal than for the easy goal. In addition, force change across the 2 goals was associated with performance change, supporting the conclusion that expectancy valence theory can predict the goal theory postulate. The valence of goal attainment was higher for the hard goal than for the easy goal. Valence change across the 2 goals was associated with performance change to a greater degree than was expectancy change, suggesting that the attained performance difference can be attributed to the valence difference. (10 ref) (PsycINFO Database Record (c) 2010 APA, all rights reserved)     

Cloning and heterologous expression of a beta-fructofuranosidase gene from Arthrobacter globiformis IFO 3062, and site-directed mutagenesis of the essential aspartic acid and glutamic acid of the active site

We have cloned the gene encoding a beta-fructofuranosidase from Arthrobacter globiformis IFO 3062, and subsequently, the gene was heterologously expressed in Escherichia coli. This beta-fructofuranosidase gene encodes a protein of 548 amino acid residues with a calculated molecular mass of 60,519 Da. We have examined the roles of three residues of A. globiformis IFO 3062 beta-fructofuranosidase by site-directed mutagenesis, and found that aspartic acid 130 and glutamic acid 392, which are two of the apparent catalytic residues, are essential for hydrolase activity. This study provides the first experimental evidence showing that these two amino acid residues of beta-fructofuranosidase play a critical role in hydrolyzing sucrose.     

Composite of Au nanoparticles and molecularly imprinted polymer as a sensing material

A molecularly imprinted polymer with immobilized Au nanoparticles (Au-MIP) is reported as a novel type of sensing material. The sensing mechanism is based upon the variable proximity of the Au nanoparticles immobilized in the imprinted polymer, which exhibits selective binding of a given analyte accompanied by swelling that causes a blue-shift in the plasmon absorption band of the immobilized Au nanoparticles. Using adrenaline as the model analyte, it was shown that molecular imprinting effectively enhanced the sensitivity and selectivity, and accordingly, Au-MIP selectively detects the analyte at 5 microM. The combination of molecular imprinting and the Au nanoparticle-based sensing system was shown to be a general strategy for constructing sensing materials in a tailor-made fashion due to wide applicability of the imprinting technique and the independence of the sensing mechanism from the analyte recognition system.     

Lipid peroxidation-derived cytotoxic aldehyde, 4-hydroxy-2-nonenal in smoked pork

The contents of 4-Hydroxy-2-nonenal (HNE), cytotoxic aldehyde, in smoked meat products (ham, bacon and sausage) were analyzed. All the samples analyzed contained HNE, although large differences in the contents between the different samples were observed. In one lot of ham (H1) and wiener sausage (WS1) a high level in HNE was observed. The changes of HNE contents of pork meats containing 0, 0.1, 0.5 and 1% Sugi wood vinegar (SWV) stored at 0?°C were also analyzed for 7 days. As an index of lipid peroxidation level, malonaldehyde (MA) contents were also analyzed in these samples. After 7 days of storage, HNE was detected only in pork meats containing 1% SWV and the level was similar to those of H1 and WS1. Judging from MA contents, SWV may act as a pro-oxidant in pork meats and HNE may accumulate in pork in which lipid peroxidation is in progress.