Advanced IC packaging for the future applications

The performance of electronic equipment is improving rapidly. Portable electronic equipment requires smaller and thinner packaging systems for saving space and miniaturization. In addition, highly integrated, high-speed applications demand improved electrical performance to minimize noise effects. As a result of these considerations, the role of IC packaging has expanded from its traditional role of protecting the integrity and performance of an IC, to being a central factor in the development of electronic system concepts. In developing the optimum system, packaging technology must be a prime design consideration to ensure optimum performance, reliability, and cost. Soldering technology and Printed Wiring Board (PWB) routing density are two of the major technological issues facing miniaturized packaging systems today. Chip Scale Package (CSP), which is a new concept in packaging technology has been introduced. This is an ideal technology to enable the design and manufacture of the next generation of electronic equipment, while overcoming many of the technological issues facing system development     

Synthesis of Heterocycle-Containing [60]Fullerene Derivatives. II.1 Recent Progress in [4 2]- and [3 2]-Cycloaddition Routes

Recent progress of synthesis of C₆₀ derivatives functionalized with hetero-cycles is reviewed, focusing attention on [4+2]- and [3+2] cycloaddition methodologies and oxidative heterocyclization.     

Recovery of serum proteins using cellulosic affinity membrane modified by immobilization of CU2+ ion

An affinity membrane was prepared from a porous cellulose membrane, and adsorption and recovery of serum proteins were investigated from the viewpoint that affinity membranes are efficacious against separation and purification of biomaterials. Into the cellulose membrane, iminodiacetate (IDA) group that acts as a ligand to metal ions was introduced (Cell–IDA membrane), and then Cu²⁺ ion was immobilized (Cell–IDA–Cu membrane). Bovine serum albumin (BSA) and γ-globulin (BγG), which are the major proteins in blood, were adopted as model proteins to be separated. The Cell–IDA–Cu membrane had large adsorption capacity for these proteins despite the low degree of modification. The amounts of proteins adsorbed on the Cell–IDA–Cu membrane increased with increasing pH, and BγG was adsorbed more than BSA. High protein recoveries from the Cell–IDA–Cu membrane were obtained. The separation of these proteins was also conducted under the optimum conditions of adsorption and recovery, and BγG was concentrated more than BSA although the initial concentration of BγG was lower than that of BSA. © 1996 John Wiley & Sons, Inc.     

Functional Characterization of 3-Aminobenzoic Acid Adenylation Enzyme PctU and UDP-N-Acetyl-d-Glucosamine: 3-Aminobenzoyl-ACP Glycosyltransferase PctL in Pactamycin Biosynthesis

Pactamycin is an antibiotic produced by Streptomyces pactum with antitumor and antimalarial properties. Pactamycin has a unique aminocyclitol core that is decorated with 3-aminoacetophenone, 6-methylsaliciate, and an N,N-dimethylcarbamoyl group. Herein, we show that the adenylation enzyme PctU activates 3-aminobenzoic acid (3ABA) with adenosine triphosphate and ligates it to the holo form of the discrete acyl carrier protein PctK to yield 3ABA-PctK. Then, 3ABA-PctK is N-glycosylated with uridine diphosphate-N-acetyl-d -glucosamine (UDP-GlcNAc) by the glycosyltransferase PctL to yield GlcNAc-3ABA-PctK. Because 3ABA is known to be a precursor of the 3-aminoacetophenone moiety, PctU appears to be a gatekeeper that selects the appropriate 3-aminobenzoate starter unit. Overall, we propose that acyl carrier protein-bound glycosylated 3ABA derivatives are biosynthetic intermediates of pactamycin biosynthesis.     

NAD+‐Dependent Dehydrogenase PctP and Pyridoxal 5′‐Phosphate Dependent Aminotransferase PctC Catalyze the First Postglycosylation Modification of the Sugar Intermediate in Pactamycin Biosynthesis

The unique five‐membered aminocyclitol core of the antitumor antibiotic pactamycin originates from d ‐glucose, so unprecedented enzymatic modifications of the sugar intermediate are involved in the biosynthesis. However, the order of the modification reactions remains elusive. Herein, we examined the timing of introduction of an amino group into certain sugar‐derived intermediates by using recombinant enzymes that were encoded in the pactamycin biosynthesis gene cluster. We found that the NAD⁺‐dependent alcohol dehydrogenase PctP and pyridoxal 5′‐phosphate dependent aminotransferase PctC converted N‐acetyl‐d ‐glucosaminyl‐3‐aminoacetophonone into 3′‐amino‐3′‐deoxy‐N‐acetyl‐d ‐glucosaminyl‐3‐aminoacetophenone. Further, N‐acetyl‐d ‐glucosaminyl‐3‐aminophenyl‐β‐oxopropanoic acid ethyl ester was converted into the corresponding 3′‐amino derivative. However, PctP did not oxidize most of the tested d ‐glucose derivatives, including UDP‐GlcNAc. Thus, modification of the GlcNAc moiety in pactamycin biosynthesis appears to occur after the glycosylation of aniline derivatives.     

Mechanism‐Based Trapping of the Quinonoid Intermediate by Using the K276R Mutant of PLP‐Dependent 3‐Aminobenzoate Synthase PctV in the Biosynthesis of Pactamycin

Mutational analysis of the pyridoxal 5′‐phosphate (PLP)‐dependent enzyme PctV was carried out to elucidate the multi‐step reaction mechanism for the formation of 3‐aminobenzoate (3‐ABA) from 3‐dehydroshikimate (3‐DSA). Introduction of mutation K276R led to the accumulation of a quinonoid intermediate with an absorption maximum at 580 nm after the reaction of pyridoxamine 5′‐phosphate (PMP) with 3‐DSA. The chemical structure of this intermediate was supported by X‐ray crystallographic analysis of the complex formed between the K276R mutant and the quinonoid intermediate. These results clearly show that a quinonoid intermediate is involved in the formation of 3‐ABA. They also indicate that Lys276 (in the active site of PctV) plays multiple roles, including acid/base catalysis during the dehydration reaction of the quinonoid intermediate.     

Thermal Stability of Hexaaluminate Film Coated on SiC Substrate for High-Temperature Catalytic Application

A coating of barium hexaaluminate (Ba_0.75Al_11.0O_17.25) on an α-SiC substrate and the thermal stability of the formed film were investigated for a high-temperature catalytic application. The film prepared by sol coating consisted of BaAl₂Si₂O₈ and α-Al₂O₃ phases and always contained many cracks or exfoliations after heating at 1200C. A hexaaluminate porous film was successfully formed by slurry coating without void formation at the interface between the film and the substrate and exfoliation due to the formation of the intermediate layer after heating at 1200°C. The microstructure of the film remained unchanged, even after heating at 1300°C.     

Steam Reforming of Methanol on Copper Catalysts Supported on Large-Surface-Area ZnAl2O3

Steam reforming of methanol on various supported Cu catalysts was examined. Supports strongly affected catalyst activity and, among the catalysts tested, Cu catalyst supported on large-surface-area ZnAl₂O₄ showed the highest activity, which, to the best of our knowledge, was higher than those for the supported catalysts reported so far. For supported Cu catalysts, two species were observed. One was a dispersed Cu species having strong interaction between Cu and support, and the other was an isolated Cu species. The activity of the former species strongly depended on supports.