Analytical calculation of muon intensities under deep sea-water

The study of the energy loss of high energy muons through different materials, such as rock and sea-water can cast light on characteristics of lepton interactions. There are less ambiguities for the values of atomic number (Z) and mass number (A) in sea-water than in rock. Muon intensities should be measured as fundamental data and as background data for searching the fluxes of neutrino. The average range energy relation in sea-water is derived. The correction factors due to the range fluctuation is also computed. By applying these results, the intensities deep under sea are converted from a given muon energy spectra at sea-level. The spectra of conventional muons from eta, K decays have sec theta enhancement. The spectrum of prompt muons from charmed particles is almost isotropic. The effect of prompt muons is examined

New measurement on photon yields from air and the application to the energy estimation of primary cosmic rays

The air fluorescence technique is used to detect ultra-high energy cosmic rays (UHECR), and to estimate their energy. Of fundamental importance is the photon yield due to excitation by electrons, in air of various densities and temperatures. After our previous report, the experiment has been continued using a Sr90 $\beta$ source to study the pressure dependence of photon yields for radiation in nitrogen and dry air. The photon yields in 15 wave bands between 300 nm and 430 nm have been determined. The total photon yield between 300 nm and 406 nm (used in most experiments) in air excited by a 0.85 MeV electron is 3.81+-0.13 (+-13 % systematics) photons per meter at 1013 hPa and 20 $^{\circ}$C. The air density and temperature dependencies of 15 wave bands are given for application to UHECR observations.Comment: 23 pages, 8 figures, LaTeX with elsart.cls, accepted by Astroparticle Physic

Characterization of bacterial acylpeptidyl-oligopeptidase

Acylpeptidyl-oligopeptidase (AOP), which has been recently identified as a novel enzyme in a periodontopathic bacterium, Porphyromonas gingivalis, removes di- and tri-peptides from N-terminally acylated polypeptides, with a preference for hydrophobic P1-position amino acid residues. To validate enzymatic properties of AOP, characteristics of two bacterial orthologues from Bacteroides dorei (BdAOP), a Gramnegative intestinal rod, and Lysinibacillus sphaericus (LsAOP), a Gram-positive soil rod, were determined. Like P. gingivalis AOP (PgAOP), two orthologues more efficiently hydrolyzed N-terminal acylated peptidyl substrates than non-acylated ones. Optimal pH was shifted from 7.0 ? 8.9 for N-acylated to 8.5 ? 9.5 for non-acylated substrates, indicating preference for non-charged hydrophobic N-terminal residues. Hydrophobic P1- and P2-position preferences were common in the three AOPs, although PgAOP preferred Leu and the others preferred Phe at the P1 position. In vitro mutagenesis demonstrated that Phe647 in PgAOP was responsible for the P1 Leu preference. In addition, bacterial AOPs commonly liberated acetyl-Ser1-Tyr2 from amelanocyte-stimulating hormone. Taken together, although these three bacterial AOPs exhibited some variations in biochemical properties, the present study demonstrated the existence of a group of exopeptidases that preferentially liberates mainly dipeptides from N-terminally acylated polypeptides with a preference for hydrophobic P1 and P2-position residues

Characterization of substrate specificity and novel autoprocessing mechanism of dipeptidase A from Prevotella intermedia

Prevotella intermedia, a gram-negative anaerobic rod, is frequently observed in subgingival polymicrobial biofilm from adults with chronic periodontitis. Peptidases in periodontopathic bacteria are considered to function as etiological reagents. Pre. intermedia OMA14 cells abundantly express an unidentified cysteine peptidase specific for Arg-4-methycoumaryl-7- amide (MCA). BAU17746 (locus tag, PIOMA14_I_1238) and BAU18827 (locus tag, PIOMA14_II_0322) emerged as candidates of this peptidase from the substrate specificity and sequence similarity with C69-family Streptococcus gordonii Arg-aminopeptidase. The recombinant form of the former solely exhibited hydrolyzing activity toward Arg-MCA, and BAU17746 possesses a 26.6% amino acid identity with the C69-family Lactobacillus helveticus dipeptidase A. It was found that BAU17746 as well as L. helveticus dipeptidase A was a P1-position Arg-specific dipeptidase A, although the L. helveticus entity, a representative of the C69 family, had been reported to be specific for Leu and Phe. The fulllength form of BAU17746 was intramolecularly processed to a mature form carrying the N-terminus of Cys15. In conclusion, the marked Arg-MCA-hydrolyzing activity in Pre. intermedia was mediated by BAU17746 belonging to the C69-family dipeptidase A, in which the mature form carries an essential cysteine at the N-terminus

Preferential dipeptide incorporation of Porphyromonas gingivalis mediated by proton-dependent oligopeptide transporter (Pot)

Multiple dipeptidyl-peptidases (DPPs) are present in the periplasmic space of Porphyromonas gingivalis, an asaccharolytic periodontopathic bacterium. Dipeptides produced by DPPs are presumed to be transported into the bacterial cells and metabolized to generate energy and cellular components. The present study aimed to identify a transporter responsible for dipeptide uptake in the bacterium. A real-time metabolic analysis demonstrated that P. gingivalis preferentially incorporated Gly-Xaa dipeptides, and then,single amino acids, tripeptides, and longer oligopeptides to lesser extents. Heterologous expression of the P. gingivalis serine/threonine transporter (SstT) (PGN_1460), oligopeptide transporter (Opt) (PGN_1518), and proton-dependent oligopeptide transporter (Pot) (PGN_0135) genes demonstrated that Escherichia coli expressing Pot exclusively incorporated Gly-Gly, while SstT managed Ser uptake and Opt was responsible for Gly-Gly-Gly uptake. Dipeptide uptake was significantly decreased in a P. gingivalis Δpot strain and further suppressed in a Δpot-Δopt double-deficient strain. In addition, the growth of the Δpot strain was markedly attenuated and the Δpot-Δopt strain scarcely grew, whereas the ΔsstT strain grew well almost like wild type. Consequently, these results demonstrate that predominant uptake of dipeptide in P. gingivalis is mostly managed by POT. We thus propose that Pot is a potential therapeutic target of periodontal disease and P. gingivalis related systemic diseases