Cambridge Reactor Design (United Kingdom)

Liquid sodium has the excellent properties as coolant of the fast breeder reactor (FBR). On the other hand, it reacts high with water and oxygen. So an innovative technology to suppress the reactivity is desired. The purpose of this study is to control the chemical reactivity of liquid sodium by dispersing the nanometer-size metallic particles (we call them Nano-particles) into liquid sodium. We focus on the atomic interaction between Nano-particles and sodium atoms. And we try to apply it to suppress the chemical reactivity of liquid sodium. Liquid sodium dispersing Nano-particles is named "Nano-fluid". Research programs of this study are the Nano-particles production, the evaluation of reactivity suppression of liquid sodium and the feasibility study to FBR plant. In this paper, the research programs and status are described. The important factors for particle production were understood. In order to evaluate the chemical reactivity of Nano-fluid the research programs were planned. The feasibility of the application of Nano-fluid to the coolant of FBR plant was evaluated preliminarily from the viewpoint of design and operation.

Nitric oxide synthase (EC 1.14.13.39) is a homodimer. Limited proteolysis has previously shown that it consists of two major domains. The C-terminal or reductase domain binds FMN, FAD and NADPH. The N-terminal or oxygenase domain is known to bind arginine, (6R)-5,6,7,8-tetrahydro-l-biopterin (tetrahydrobiopterin) and haem. The exact residues of the inducible nitric oxide synthase (iNOS) protein involved in binding to these molecules have yet to be identified, although the haem moiety is known to be co-ordinated through a cysteine thiolate ligand. We have expressed two forms of the haem-binding domain of human iNOS (residues 1-504 and 59-504) in Escherichia coli as glutathione S-transferase (GST) fusion proteins. The iNOS 1-504 and 59-504 fusion proteins bound similar amounts of haem, Nomega-nitro-l-arginine (nitroarginine) and tetrahydrobiopterin, showing that the first 58 residues are not required for binding these factors. Using site-directed mutagenesis we have mutated Cys-200, Cys-217, Cys-228, Cys-290, Cys-384 and Cys-457 to alanine residues within the iNOS 59-504 haem-binding domain. Mutation of Cys-200 resulted in a complete loss of haem, nitroarginine and tetrahydrobiopterin binding. Mutants of Cys-217, Cys-228, Cys-290, Cys-384 or Cys-457 showed no effect on the haem content of the fusion protein, no effect on the reduced CO spectral peak (444 nm) and were able to bind nitroarginine and tetrahydrobiopterin at levels equivalent to the wild-type fusion protein. After removal of the GST polypeptide, the wild-type iNOS 59-504 domain was dimeric, whereas the C200A mutant form was monomeric. When the mutated domains were incorporated into a reconstructed full-length iNOS protein expressed in Xenopus oocytes, only the Cys-200 mutant showed a loss of catalytic activity: all the other mutant iNOS proteins showed near wild-type enzymic activity. From this systematic approach we conclude that although Cys-217, Cys-228, Cys-290, Cys-384 and Cys-457 are conserved in all three NOS isoforms they are not essential for cofactor or substrate binding or for enzymic activity of iNOS, and that Cys-200 provides the proximal thiolate ligand for haem binding in human iNOS.

The COMMIX-LAR/P computer program is designed for analyzing the steady-state and transient aspects of single-phase fluid flow and heat transfer in three spatial dimensions. This version is an extension of the modeling in COMMIX-lA to include multiple fluids in physically separate regions of the computational domain, modeling descriptions for pumps, radiation heat transfer between surfaces of the solids which are embedded in or surround the fluid, a keg model for fluid turbulence, and improved numerical techniques. The porous-medium formulation in COMMIX allows the program to be applied to a wide range of problems involving both simple and complex geometrical arrangements. The internal aspects of the COMMIX-LAR/P program are presented, covering descriptions of subprograms, variables, and files.

The object of this paper discusses the design review of the boron carbide safety rod for the Westinghouse Savannah River Company. This paper reviewed information presented by personnel of the Savannah River Laboratory (SRL) Equipment Engineering Section, SRL Materials Technology Section and Reactor Materials Engineering and Technology. From this report, views, opinions and recommendations were made on the safety rod from materials testing to production.

this difference increased as Pr decreased. It was also found that the perturbation method of solution of the free-convection boundary-layer equations becomes useless for small values of Pr because of the slow convergence of the series. The results obtained by the integral method were in good agreement with those calculated by the perturbation method for Pr approximately 1 and 0.1 < xi < 1 only; they deviated considerably for smaller values of xi . (auth)

given. Calculations are presented for a fluid whose Prandtl number is one, as well as for molten Pyrex glass. (auth)