An in-phantom comparison of neutron fields for BNCT

Previously, the authors have developed the in-phantom neutron field assessment parameters T and D (Tumor) for the evaluation of epithermal neutron fields for use in BNCT. These parameters are based on an energy-spectrum-dependent neutron normal-tissue RBE and the treatment planning methodology of Gahbauer and his co-workers, which includes the effects of dose fractionation. In this paper, these neutron field assessment parameters were applied to The Ohio State University (OSU) design of an Accelerator Based Neutron Source (ABNS) (hereafter called the OSU-ABNS) and the Brookhaven Medical Research Reactor (BMRR) epithermal neutron beam (hereafter called the BMRR-ENB), in order to judge the suitability of the OSU-ABNS for BNCT. The BMRR-ENB was chosen as the basis for comparison because it is presently being used in human clinical trials of BNCT and because it is the standard to which other neutron beams are most often compared

Evaluation of coverage of enriched UF{sub 6} cylinder storage lots by existing criticality accident alarms

The Portsmouth Gaseous Diffusion Plant (PORTS) is leased from the US Department of Energy (DOE) by the United States Enrichment Corporation (USEC), a government corporation formed in 1993. PORTS is in transition from regulation by DOE to regulation by the Nuclear Regulatory Commission (NRC). One regulation is 10 CFR Part 76.89, which requires that criticality alarm systems be provided for the site. PORTS originally installed criticality accident alarm systems in all building for which nuclear criticality accidents were credible. Currently, however, alarm systems are not installed in the enriched uranium hexafluoride (UF{sub 6}) cylinder storage lots. This report analyzes and documents the extent to which enriched UF{sub 6} cylinder storage lots at PORTS are covered by criticality detectors and alarms currently installed in adjacent buildings. Monte Carlo calculations are performed on simplified models of the cylinder storage lots and adjacent buildings. The storage lots modelled are X-745B, X-745C, X745D, X-745E, and X-745F. The criticality detectors modelled are located in building X-343, the building X-344A/X-342A complex, and portions of building X-330. These criticality detectors are those located closest to the cylinder storage lots. Results of this analysis indicate that the existing criticality detectors currently installed at PORTS are largely ineffective in detecting neutron radiation from criticality accidents in most of the cylinder storage lots at PORTS, except sometimes along portions of their peripheries

Role of C-reactive protein in complement-mediated hemolysis in Malaria

HumanC-reactive protein (CRP) is a clinically important classical acute phase protein. Although CRP has been reported to bind with many nucleated cells, the direct binding of CRP to erythrocytes in diseases remains largely unexplored. The main focus of the present studywas to investigate the binding of disease-specific CRP to erythrocytes of same patients. Distinct molecular variant of disease-specific CRP was affinity purified from sera of malaria patients (CRPMal). This CRP showed strong binding with malaria erythrocytes (RBCMal) as confirmed by flow cytometric analysis (FACS), enzyme-linked immunosorbent assays (ELISA), and radio binding assays. Calcium and phosphoryl choline (PC) were found to be essential for this interaction.A2.3-fold increased binding of induced CRP to RBCMal as compared to normal erythrocytes (RBCN) confirmed disease-specificity. Preincubation of RBCMal with unconjugated CRP showed 3–5 fold inhibition. The association constant of CRP and RBCMal was 4.7 × 106 cpm/μg with the corresponding number of receptors/ cell being 4.3 × 105. The effector function of CRPMal has been demonstrated by its potency to activate the complement pathway. An optimal dose of 10 μg/ml of CRP induced three-fold higher hemolysis of patient erythrocytes as compared to RBCN. These studies provide direct evidence for an important phagocytic functional interaction of this acutephase protein by triggering the CRP-complement pathway after the binding of CRPMal with RBCMal. Hemolysis as triggered by this pathway may be one of the causative factors of anemia, a common clinical manifestation of this diseas