ABSTRACT
The King AbdulAziz City for Science & Technology in the Kingdom of Saudi Arabia plans to build a 10âMeV, 15âkW linear accelerator (LINAC) for electron beam and X-ray. The accelerator will be supplied by EB Tech, Republic of Korea, and the design and construction of the accelerator building will be conducted in the cooperation with EB Tech. This report presents the shielding analysis of the accelerator building using the Monte Carlo N-Particle Transport Code (MCNP). In order to improve the accuracy in estimating deep radiation penetration and to reduce computation time, various variance reduction techniques, including the weight window (WW) method, the deterministic transport (DXTRAN) spheres were considered. Radiation levels were estimated at selected locations in the shielding facility running MCNP6 for particle histories up to 1.0×10+8. The final results indicated that the calculated doses at all selected detector locations met the dose requirement of 50âmSv/yr, which is the United State Nuclear Regulatory Commission (U.S. NRC) requirement.
Subject(s)
Particle Accelerators , Radiation Protection , Electrons , Equipment Design , Monte Carlo Method , Radiation Protection/instrumentation , Radiation Protection/methods , X-RaysABSTRACT
An Escherichia coli expression system has been constructed for production of biologically active recombinant histone H1.5. A process of fermentation and purification method at a large scale has been developed. Recombinant histone H1.5 was released from the high density cultured cells by high-pressure homogenization. For an efficient removal of cell debris and partial purification of basic histone H1.5 in a single step, the whole cell lysates were directly loaded onto an expanded bed column packed with the strong cation exchanger (Streamline SP). Complete removal of various impurities was achieved by a combination of hydroxyapatite chromatography and the following cation exchange chromatography with high grade strong cation exchanger (POROS 20 HS), and finally endotoxins were removed by ultrafiltration using a 100-kDa cut-off membrane, which gave the level of endotoxin below 0.5 EU/mg. The molecular mass of the recombinant histone H1.5 analyzed by MALDI-TOF-MS, and the N-terminal amino acid sequences were in good agreement with the authentic histone H1.5. The whole process gave highly purified recombinant histone H1.5 at a high yield, compared to the conventional process.
Subject(s)
Escherichia coli/chemistry , Escherichia coli/genetics , Histones/isolation & purification , Recombinant Proteins/isolation & purification , Chromatography, High Pressure Liquid , Chromatography, Ion Exchange , Electrophoresis, Polyacrylamide Gel , Endotoxins/analysis , Histones/chemistry , Humans , Hydroxyapatites , Recombinant Proteins/chemistry , UltrafiltrationABSTRACT
A magainin derivative, designated MSI-344, was produced in Escherichia coli as fusion protein, by utilizing a truncated amidophsphoribosyltransferase of E. coli as a fusion partner. Bacterial cells transformed with the gene encoding the fusion protein were grown to a high cell density and induced with isopropyl-1-thio-b-D-galatoside (IPTG) to initiate product expression. The fusion protein was accumulated into cytoplasmic inclusion body and recombinant MSI-344 was released from the fusion partner by hydroxylamine treatment. Following cleavage of the fusion protein with hydroxylamine, the released MSI-344 was purified to homogeneity by cationic exchange chromatography. The final purity was at least 95% by reversed-phase high performance liquid chromatography (RP-HPLC). Purified recombinant MSI-344 was found to be indistinguishable from the synthetic peptide determined by amino acid sequences and antimicrobial activity assay.
