Delayed particles in EAS at Akeno

Using two 2.25 square meter fast scintillation detectors, delayed particles in cosmic ray showers (CRS) have been observed at Akeno Observatory. These are set under 1 m concrete and 2.5 cm lead plates respectively. About 2500 CRS are analyzed. The lateral distribution of delayed particles for the CRS size 10 to the 7th power is flatter than that for to the 7th power. The lateral density of delayed particles is almost constant for the size range 2.2 X 10 to the 5th power approx. 10 to the 7th power and increases rapidly above 10 to the 7th power. These facts may suggest change of nuclear interaction at 10 to the 7th power and substantially the existence of heavy particles with long life

Observation of EAS using a large water tank

Using a large water tank (30 m in diameter, 4.5 m in depth) transition of extensive air showers (EAS) was investigated at Taro (200 m above sea level). There are set 150,0.4 sq m proportional counters on the bottom of the water tank. A conventional EAS array of 25 plastic scintillation detectors was arranged within several tens meter from the water tank. A proportional counter (10x10x200 cc x2) is made of a square shaped pipe of iron. Tungsten wire (100 mu m phi) is stretched tight in the center of the counter. A gas mixture of 90% argon and 10% methane is used at 760 mmHg. About 3000 EAS were obtained through 1 m of water since 1984

Subduction initiation and ophiolite crust: new insights from IODP drilling

International Ocean Discovery Program (IODP) Expedition 352 recovered a high-fidelity record of volcanism related to subduction initiation in the Bonin fore-arc. Two sites (U1440 and U1441) located in deep water nearer to the trench recovered basalts and related rocks; two sites (U1439 and U1442) located in shallower water further from the trench recovered boninites and related rocks. Drilling in both areas ended in dolerites inferred to be sheeted intrusive rocks. The basalts apparently erupted immediately after subduction initiation and have compositions similar to those of the most depleted basalts generated by rapid sea-floor spreading at mid-ocean ridges, with little or no slab input. Subsequent melting to generate boninites involved more depleted mantle and hotter and deeper subducted components as subduction progressed and volcanism migrated away from the trench. This volcanic sequence is akin to that recorded by many ophiolites, supporting a direct link between subduction initiation, fore-arc spreading, and ophiolite genesis

Functional Characterization of a First Avian Cytochrome P450 of the CYP2D Subfamily (CYP2D49)

The CYP2D family members are instrumental in the metabolism of 20–25% of commonly prescribed drugs. Although many CYP2D isoforms have been well characterized in other animal models, research concerning the chicken CYP2Ds is limited. In this study, a cDNA encoding a novel CYP2D enzyme (CYP2D49) was cloned from the chicken liver for the first time. The CYP2D49 cDNA contained an open reading frame of 502 amino acids that shared 52%–57% identities with other CYP2Ds. The gene structure and neighboring genes of CYP2D49 are conserved and similar to those of human CYP2D6. Additionally, similar to human CYP2D6, CYP2D49 is un-inducible in the liver and expressed predominantly in the liver, kidney and small intestine, with detectable levels in several other tissues. Metabolic assays of the CYP2D49 protein heterologously expressed in E. coli and Hela cells indicated that CYP2D49 metabolized the human CYP2D6 substrate, bufuralol, but not debrisoquine. Moreover, quinidine, a potent inhibitor of human CYP2D6, only inhibited the bufuralol 1′-hydroxylation activity of CYP2D49 to a negligible degree. All these results indicated that CYP2D49 had functional characteristics similar to those of human CYP2D6 but measurably differed in the debrisoquine 4′-hydroxylation and quinidine inhibitory profile. Further structure-function investigations that employed site-directed mutagenesis and circular dichroism spectroscopy identified the importance of Val-126, Glu-222, Asp-306, Phe-486 and Phe-488 in keeping the enzymatic activity of CYP2D49 toward bufuralol as well as the importance of Asp-306, Phe-486 and Phe-488 in maintaining the conformation of CYP2D49 protein. The current study is only the first step in characterizing the metabolic mechanism of CYP2D49; further studies are still required