Interlocking design, programmable laser manufacturing and testing for architectured ceramics.

Tough and impact-resistant ceramic systems offer a wide range of remarkable opportunities beyond those offered by the conventional brittle ceramics. However, despite their promise, the availability of traditional manufacturing technique for fabricating such advanced ceramic structures in a highly controllable and scalable manner poses a significant manufacturing bottleneck. In this study, a precise and programmable laser manufacturing system was used to manufacture topologically interlocking ceramics. This manufacturing strategy offers feasible mechanisms for a precise material architecture and quantitative process control, particularly when scalability is considered. An optimized material removal method that approaches near-net shaping was employed to fabricate topologically interlocking ceramic systems (load-carrying assemblies of building blocks interacting by contact and friction) with different architectures (i.e., interlocking angles and building block sizes) subjected to low-velocity impact conditions. These impacts were evaluated using 3D digital image correlation. The optimal interlocked ceramics exhibited a higher deformation (up to 310%) than the other interlocked ones advantageous for flexible protections. Their performance was tuned by controlling the interlocking angle and block size, adjusting the frictional sliding, and minimizing damage to the building blocks. In addition, the developed subtractive manufacturing technique leads to the fabrication of tough, impact-resistant, damage-tolerant ceramic systems with excellent versatility and scalability.

Comparative protein binding of taxotere and SID530, a new docetaxel formulation with hydroxypropyl-beta-cyclodextrin, in human plasma in vitro.

The purpose of this study was to evaluate the plasma-protein binding of docetaxel in two different formulations, Taxotere and SID530, a new docetaxel formulation with hydroxypropyl-beta-cyclodextrin (HP-beta-CD), in human plasma in vitro, using equilibrium dialysis. Unbound docetaxel concentration in the human plasma was determined by LC-MS/MS analysis. SID530 showed a plasma-protein binding profile comparable to that of Taxotere in the clinically relevant concentration range of docetaxel. In both formulations, the unbound fraction of docetaxel increased in a concentration-dependent biphasic manner. The resulting data indicate that the excipient used in SID530, HP-beta-CD, generates similar effects as polysorbate 80 of Taxotere in terms of plasma-protein binding of docetaxel.

Short-term distributions of reduced sulfur compounds in the ambient air surrounding a large landfill facility.

In order to explore the environmental behavior of reduced sulfur compounds (RSC) as malodorous components emitted from diverse source processes, the distribution characteristics of four sulfur (S) compounds - hydrogen sulfide (H2S), methyl mercaptan (CH3SH), dimethyl sulfide (DMS: (CH3)2S), and dimethyl disulfide (DMDS: (CH3)2S2) - were investigated in a municipal landfill area. In the course of this study, their ambient concentration levels were measured during two time periods from 13 individual spots selected as a function of distance from the center of the landfill site. The results generally indicated the absolute dominance of H2S over the other S compounds investigated (up to 5 km radius) such that their mean values were found as 1415 (H2S), 148 (DMS), 20.6 (CH3SH), and 14.4 ppt (DMDS). When our data were compared in terms of either varying distance from the source or relationship with meteorological conditions, the H2S data sets were most evident to reflect the potential effects of strong source processes in the landfill environment, relative to other S gases (or to volatile organic compounds measured concurrently). The results of this study further indicated the relatively good correspondence between the measured H2S concentration level and humans' intuitive sensory of odor and nuisance.

A second form of phenylalanine ammonia-lyase from leaf mustard.

Phenylalanine ammonia-lyase (PAL, EC 4.3.1.5) catalyzes the elimination of ammonium ion from L-phenylalanine in a variety of plants and fungal species. PAL was previously purified and characterized from leaf mustard in our laboratory. In the present study, we purified a second phenylalanine ammonia-lyase (PAL II) from leaf mustard by a combination of ion exchange chromatography and gel filtration. PAL I and PAL II migrate at a different rate on native polyacrylamide gel electrophoresis. It consists of four subunits, each having the molecular mass of about 37,000 Da. Its isoelectric point and Km value for L-phenylalanine were found to be 5.4 and 3.8 x 10(-5)M, respectively. The purified enzyme has an optimum pH and temperature of 8 and 45 degree C, respectively. It is activated about 2-fold by caffeic acid (1 mM), whereas it is inhibited to 15% by Zn2+ (1 mM). However, the physiological role of PAL II remains unknown.

Purification and characterization of glutaredoxin from Cryptococcus neoformans.

Glutaredoxin, also known as thioltransferase, was purified from Cryptococcus neoformans by procedures including DEAE-cellulose ion exchange chromatography, Q-Sepharose ion-exchange chromatography, and gel filtration on Sephadex G-50. Its purity was confirmed by SDS-polyacrylamide gel electrophoresis and its molecular weight was estimated to be 12,000 Da. The purified enzyme has a K(m) value of 1.03 mM with 2-hydroxyethyl disulfide as a substrate. The enzyme also utilizes L-sulfocysteine, L-cystine, and bovine serum albumin as substrates in the presence of reduced glutathione. The enzyme has K(m) values of 0.34-2.50 mM for these substrates. It was greatly activated by thiol compounds such as reduced glutathione, dithiothreitol, L-cysteine and beta-mercaptoethanol. It is partially inactivated at 60 degrees C or higher temperatures. It plays an important role in thiol-disulfide exchange in Cryptococcus neoformans.

Expression of the Escherichia coli thioredoxin gene is negatively regulated by cyclic AMP.

Regulation of the Escherichia coli thioredoxin gene (trxA) was studied using trxA-lac translational fusion constructed in the vector pMC1403. Synthesis of beta-galactosidase from the trxA-lac fusion was found to be repressed in the presence of lactose. A switch of carbon source from glucose to lactose and an addition of cyclic AMP (cAMP) caused a decrease in beta-galactosidase synthesis from the trxA-lac fusion. The repression effect of exogenous cAMP was not observed in the crp mutant strain. The beta-galactosidase synthesis from the trxA-lac fusion lacking a plausible cAMP-CRP binding site was not lowered in the presence of lactose or in the addition of cAMP. Expression of the chromosomal trxA gene was reduced by exogenous cAMP. These findings indicate that the expression of the trxA gene is controlled by cAMP in a negative manner.

Identification of a third thioredoxin gene from Corynebacterium nephridii.

We identified and sequenced a gene encoding a third thioredoxin (C3) from Corynebacterium nephridii. The determined nucleotide sequence encodes a thioredoxin of 145 amino acid residues, which is larger than most thioredoxins found in microbial cells and contains 6 cysteine residues. C. nephridii thioredoxin C3 is able to serve as a subunit of T7 DNA polymerase. C. nephridii is the first nonphotosynthetic procaryotic organism known to carry three different thioredoxins.