防犯のために取り組むのはどのような人々か : 社会学的研究における議論を再考する

本稿では、2015年に警察庁が実施した「全国統一治安意識調査」のデータを用いて、自主防犯活動への参加、防犯行動の説明要因を分析した。結果から、以下が明らかになった。 男性よりも女性のほうが自主防犯活動に参加しない傾向にあるが、小学6年生以下の子どもと同居する場合は男女による参加傾向の違いはない。警察への信頼度の高さ、近所づきあい、無秩序の程度の高さなどは、自主防犯活動への参加と関連している。凶悪犯罪に対する不安は、自主防犯活動への参加とは有意な関連は見られない。 女性は男性に比べて、防犯行動を行っている。警察への信頼度の高さ、凶悪犯罪に対する不安、身体犯被害の経験などは防犯行動と関連している。 The present paper examines the correlates of membership in neighborhood watch activities and anti-crime behavior by using data from the National Uniform Subjective Security Survey conducted by the National Police Agency. The results are as follows: 1) Women are less likely to participate in neighborhood watch activities, except for those living with a sixth-grade child or younger. 2) Confidence in police, social ties, and incivility relate to membership in neighborhood watch activities. 3) Fear of heinous crimes has no significant effect on membership in neighborhood watch activities. 4) Women are more likely to be serious about anti-crime behavior. 5) Confidence in police as well as fear of heinous crimes and personal victimization relate to anti-crime behavior.1．はじめに 2．先行研究の検討と分析枠組み 3．結果と考察 4．終わりにtextapplication/pdfdepartmental bulletin pape

A research on cooperative problem solving learning in mathematics education : construction learning processes and object of evaluation

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Observation of B+→pp̅π+, B0→pp̅K0, and B+→pp̅K*+

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APPROXIMATION OF AN ENTIRE FUNCTION

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Apparent Half-Lives of Chlorinated-Perfluorooctane Sulfonate and Perfluorooctane Sulfonate Isomers in Aviation Firefighters

Elevated levels of perfluorooctane sulfonate (PFOS) and elevated detection frequency of chloro-substituted PFOS have been reported in Australian firefighters with historical exposure to aqueous-film forming foam (AFFF). The aim of this study is to estimate the apparent half-lives of Cl–PFOS and PFOS isomers in firefighters following the end of exposure to 3M-AFFF. Paired serum samples from 120 firefighters, collected approximately five years apart, were analyzed for 8-Cl–PFOS (8-chloroperfluoro-1-octanesulfonic acid) and PFOS isomers via targeted LC–MS/MS. Apparent half-life was estimated by assuming a first order-elimination model. Cl–PFOS was detected in 93% of all initial serum samples

Pf332 is synthesized and trafficked within the parasite as a sodium carbonate extractable protein.

<p>(<b>A</b>) Schematic representation of the experiment. Parasitized RBC at 6–10 h p.i. were mock-treated (BFA−) or BFA treated (BFA+) for 20 h (until reaching approximately 28–32 h p.i.). To verify that BFA inhibited protein export, BFA+ and BFA− pRBC at 28–32 h p.i were collected for IFA, as described in 5B. In order to analyze in what physiological state Pf332 was synthesized and trafficked within the parasite, BFA+ pRBC at 28–32 h p.i. were lysed with saponin and trypsin-treated to remove any exported protein. Intact parasites were subsequently collected and proteins extracted, as described in 5C. (<b>B</b>) Air-dried monolayers of BFA+ and BFA− pRBC were probed with monoclonal anti-Pf332-DBL (red) and polyclonal anti-PfSeryl-tRNA synthetase antibodies (green), or polyclonal anti-Pf332-E200 (red) and polyclonal anti-PfSBP1 antibodies (green). The parasite was counterstained with DAPI (blue). Scale bar indicates 5 µm. (<b>C</b>) Intact parasites were lysed in a hypotonic buffer and the resulting protein extract was separated by centrifugation into a soluble supernatant and an insoluble pellet. The supernatant was analyzed as water-soluble proteins (SN1). The membrane fraction was extracted with alkaline sodium carbonate and the resulting protein extract was separated by centrifugation into a soluble supernatant and an insoluble pellet. The supernatant was analyzed as sodium carbonate released peripheral proteins (SN2), and the pellet was analyzed as insoluble integral membrane proteins (P). Extracts from 3×10⁶ pRBC were examined per lane by Western blotting using monoclonal anti-Pf332-DBL, polyclonal anti-PfSBP1, and polyclonal anti-PfSeryl-tRNA synthetase antibodies. Full-length Pf332 is marked with an asterisk. (BFA: Brefeldin-A, IFA: immunofluorescence microscopy assay).</p

研究速報 : メカニカルファスナーにより取付けられた耐震補強ブレースのハイブリッド地震応答実験

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Pf332 is not exposed at the red blood cell surface.

<p>(<b>A</b>) Surface expression of Pf332 was studied in live intact (left panel) or RBC plasma membrane permeabilized (EqtII-treated, right panel) schizont-stage FCR3S1.2 pRBC by flow cytometry. To detect Pf332, monoclonal mouse anti-Pf332-DBL, polyclonal rat anti-Pf332-DBL (N-terminus of Pf332), and polyclonal rabbit anti-Pf332-EB200 (C-terminus of Pf332) were used. As a marker for a positive surface expression, a monoclonal mouse antibody towards the ectodomain of the PfEMP1 variant expressed by the FCR3S1.2 parasite strain was used (anti-PfEMP1-NTSDBL1α). As a marker for an intracellular localization, a mouse monoclonal antibody towards the intracellular acidic terminal segment (ATS) of PfEMP1 was used. Non-immune mouse immunoglobulin G (IgG) and pre-immune rabbit/rat sera were used as negative controls and are displayed in red. Specific anti-Pf332 and anti-PfEMP1 antibodies are displayed in blue. (<b>B</b>) Intact schizont-stage HB3 pRBC were treated with (+) or without (−) trypsin, and whole cell lysates were analyzed by Western blotting using monoclonal anti-PfEMP1-ATS (left) or polyclonal anti-Pf332 antibodies (C-terminus, right). Full-length PfEMP1 and Pf332 are indicated with asterisks. Surface-exposed PfEMP1 is cleaved by trypsin, resulting in a truncated polypeptide migrating at approximately 80 kDa (black arrow head). The blot was also probed with monoclonal mouse anti-spectrin antibodies to confirm equal loading and to show that the anti-PfEMP1-ATS antibody cross-reacts with spectrin (middle).</p

<em>Plasmodium falciparum</em> Antigen 332 Is a Resident Peripheral Membrane Protein of Maurer's Clefts

<div><p>During the intraerythrocytic development of <em>Plasmodium falciparum</em>, the malaria parasite remodels the host cell cytosol by inducing membranous structures termed Maurer's clefts and inserting parasite proteins into the red blood cell cytoskeleton and plasma membrane. Pf332 is the largest known asexual malaria antigen that is exported into the red blood cell cytosol where it associates with Maurer's clefts. In the current work, we have utilized a set of different biochemical assays to analyze the solubility of the endogenous Pf332 molecule during its trafficking from the endoplasmic reticulum within the parasite to the host cell cytosol. Solubilization studies demonstrate that Pf332 is synthesized and trafficked within the parasite as a peripheral membrane protein, which after export into the host cell cytosol associates with the cytoplasmic side of Maurer's clefts in a peripheral manner. By immunofluorescence microscopy and flow cytometry, we show that Pf332 persists in close association with Maurer's clefts throughout trophozoite maturation and schizogony, and does not become exposed at the host cell surface. Our data also indicate that Pf332 interacts with the host cell cytoskeleton, but only in very mature parasite stages. Thus, the present study describes Pf332 as a resident peripheral membrane protein of Maurer's clefts and suggests that the antigen participates in host cytoskeleton modifications at completion of the intraerythrocytic developmental cycle.</p> </div

Proposed model for the subcellular localization of the Pf332 antigen.

<p>We propose that Pf332 is a resident peripheral membrane protein of Maurer's clefts, which associates with the cytoplasmic side of the clefts. At completion of the intraerythrocytic developmental cycle, Pf332 interacts with the host cell cytoskeleton. For simplicity, only antigens of relevance for this study are depicted. Pf332 is displayed in red. (RBC PM: red blood cell plasma membrane).</p