Oversize single-mode H-guide

A new type of H-guide is proposed which is more than ten times as large as the conventional H-guide in transverse dimensions, but can operate in a single mode. A single order of magnitude reduction in attenuation over the single-strip and double-strip H-guide can be achieved with this oversize H-guide     

Giant hepatic biloma following transcatheter oily chemoembolization in a patient with hepatic metastases from malignant pheochromocytoma

A 48-year-old woman developed hepatic metastases from malignant pheochromocytoma resected 8 years previously. Angiography revealed multiple tumor stains in the liver. Transcatheter oily chemoembolization using styrenomaleic acid neocarzinostatin and iodized oil was performed. The patient complained of severe right upper quadrant pain immediately following the transcatheter oily chemoembolization. Necrotizing cholecystitis developed on the 4th day post-transcatheter oily chemoembolization, hepatic infarction on the 12th day, and a biloma on the 19th day. Despite the administration of antibiotics and percutaneous transhepatic drainage, neither the volume of drainage nor the size of the biloma decreased. Biliary reconstruction was performed using a metallic stent, which decreased the size of the biloma.     

Effect of heat-treatment on the hydrogen sensitivity of ZnO thin films loaded with palladium salts

Porous ZnO thin films were impregnated with palladium salts from their aqueous solutions, and the effects of heat-treatments on the appearence of the hydrogen sensitivity were investigated. In the course of the impregnation of PdCl₂, a ZnCl₂·4Zn(OH)₂ phase is formed in a surface region which retards the appearence of the hydrogen sensitivities. By heating the sample at 140–200 °C, this phase is decomposed but the impregnated PdCl₂ is not decomposed, and a remarkable hydrogen sensitivity appears even at room temperature. Similar situations hold in the loading of other kind of palladium salts, although the magnitude of the sensitivity is different between different kinds of loaded salts. The mechanisms of the appearence of the hydrogen sensitivity and of the loss of the sensitivity caused by the heat-treatment at higher temperatures are discussed.     

Pore formation and translocation of melittin

Ferritin (Ft) plays an important role in cellular iron metabolism. It can store substantial amounts of iron in a nontoxic soluble form. However, its ability to donate iron for cellular needs, in particular for hemoglobin (Hb) synthesis in human erythroid cells, is still controversial. We studied the role of intracellular Ft-iron in Hb synthesis and the involvement of lysosomal proteolysis in iron release from Ft. Ft-iron release and its subsequent incorporation into heme was investigated in normal human erythroid precursors developing in culture. Dual staining flow cytometry with antibody (Ab)-specific for Ft and for Hb showed a decrease in cellular Ft content in erythroid cells during their maturation. Cellular Ft-iron participation in heme synthesis was studied by labeling cells with 59Fe. Cells were incubated with 59Fe-labeled human diferric transferrin (Tf), then chased, and intracellular radioiron distribution between Ft and Hb was determined on subsequent days by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and/or Ft immunoprecipitation and heme extraction. On day 6, most of the 59Fe accumulated in Ft. Thereafter, a progressive decrease of radioiron in Ft and a corresponding increase of the label in Hb was observed. Inhibition of heme synthesis with succinylacetone caused radioiron to remain in Ft and prevented its redistribution. Addition of unlabeled diferric Tf to the culture medium did not prevent radioiron from appearing in Hb. Chloroquine repression of lysosomal function prevented radio-iron redistribution between Ft and Hb. Inhibition of proteolysis by chymostatin and/or leupeptin led to Ft-protein accumulation in the cells and also prevented radioiron transfer from Ft to Hb. The results of the present study suggest that intracellular Ft donates iron for heme synthesis and that proteolytic Ft degradation in a lysosomal-like compartment is necessary for iron release and its transfer to heme.     

A simple stochastic control problem with anticipation

We consider in this note a particular case of the problem of stochastic optimal control when the state noise is a Brownian motion process(w_{z}), z in [0,1]and the value of (w1) is known a priori. An example of application is given in terms of spatial noises.     

GTP cyclohydrolase I feedback regulatory protein is a pentamer of identical subunits. Purification, cDNA cloning, and bacterial expression

GTP cyclohydrolase I feedback regulatory protein (GFRP) mediates feedback inhibition of GTP cyclohydrolase I activity by tetrahydrobiopterin and also mediates the stimulatory effect of phenylalanine on the enzyme activity. To characterize the molecular structure of GFRP, we have purified it from rat liver using an efficient step of affinity chromatography and isolated cDNA clones, based on partial amino acid sequences of peptides derived from purified GFRP. Comparison between the amino acid sequence deduced from the cDNA and the N-terminal amino acid sequence of purified GFRP showed that the mature form of GFRP consists of 83 amino acid residues with a calculated Mr of 9,542. The isolated GFRP cDNA was expressed in Escherichia coli as a fusion protein with six consecutive histidine residues at its N terminus. The fusion protein was affinity-purified and digested with thrombin to remove the histidine tag. The resulting recombinant GFRP showed kinetic properties similar to those of GFRP purified from rat liver. Cross-linking experiments using dimethyl suberimidate indicated that GFRP was a pentamer of 52 kDa. Sedimentation equilibrium measurements confirmed the pentameric structure of GFRP by giving an average Mr of 49,734, which is 5 times the calculated molecular weight of the recombinant GFRP polypeptide. Based on the pentameric structure of GFRP, we have proposed a model for the quaternary structure of GFRP and GTP cyclohydrolase I complexes.     

Anion-induced conformational transition of poly(l-arginine) and its two homologues

The interaction of various anions with poly(l-arginine) and its two homologues, poly(l-homoarginine) and poly(l-α-amino-γ-guanidinobutyric acid), has been studied in the neutral pH region. These polypeptides were found to change their conformations from coil to helix due to I^?, ClO^?₄ and SCN^?, and among them poly(l-homoarginine) and poly(l-arginine) were found to change conformation at smaller concentrations of the anions than poly(l-lysine). The helix of poly(l-homoarginine) was induced in the lyotropic series of the counteranions. Using the van't Hoff enthalpies for the transition of the polypeptides and the transition enthalpies obtained from calorimetry, the various thermodynamic parameters of the transitions were calculated by use of a theory based on the non-specific and the specific binding interactions of the anions with the charged sites on the polypeptides. The binding constants of ClO^?₄ and SCN^? with poly(l-homoarginine) and poly(l-arginine) were found to be four times as large as those with poly(l-lysine). The free energy changes of the transitions from coil to helix of poly(l-homoarginine) and poly(l-arginine) were found to be more negative than that of poly(l-lysine). From these results, the guanidinium ion can be concluded to form easily the ion pair with the anions on the polymer surface, thus allowing poly(l-homoarginine) and poly(l-arginine) to change their conformations at smaller concentrations of the anions than poly(l-lysine).