Search PubMedSearch

PubMed · 643920

A proposal concerning the absorbed dose conversion factor.

Abstract

New definitions of the absorbed dose conversion factors Clambda and CE are proposed. The absorbed dose in water is given by the product of absorbed dose conversion factor, exposure calibration factor, ionisation chamber reading, cap displacement correction factor and perturbation correction factor. At exposure calibration the material of the build-up cap must be the same as that of the chamber wall. An ionisation chamber of which the wall material is water-equivalent or air-equivalent may be used. In the latter case the wall must be thin. For these two cases absorbed dose conversion factors are introduced and it is recommended that either of the two sets should be adopted. Furthermore, if the chamber wall is neither water- nor air-equivalent, the factor by which these currently defines values should be mutliplied is also given: again the wall must be thin. The ICRU definitions of Clambda and CE are inconsistent, as recently pointed out, while the definitions presented here are consistent.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

A Shiragai. 1978. A proposal concerning the absorbed dose conversion factor.. https://doi.org/10.1088/0031-9155%2F23%2F2%2F003

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Technical note: reconstructing dose distributions from manually planned electron boosts in breast radiotherapy.

PURPOSE: In breast radiotherapy, delivery of manually-calculated electron boosts limits retrospective dose-response analyses as dose distribution is unavailable. This work evaluates the feasibility of reconstructing dose distributions from manually planned electron boosts in breast-conserving radiotherapy. METHODS: Only 72 out of 198 breast cancer patients had complete stored dose distributions from sequential electron boosts in the REQUITE study. Arbitrary data from 70/72 patients were used to develop and validate dose reconstruction method. Twenty patients were used to determine optimal parameters for Monte-Carlo-based (MC) electron dose reconstruction on RayStation (v.11B-R), considering CT-calibration curve, MC-history number, andcalculation grid resolution. Remaining 50 patients were used to quantify dose reconstruction accuracy. The similarity between reconstructed and stored dose was evaluated using 3D-gamma index and dosimetric parameters extracted from breast and tumour bed contours. Dose difference location was evaluated using dose-location histogram. RESULTS: Calculation grid resolution significantly impacted electron dose distribution (p&#xa0;<&#xa0;0.01), where the finest grid (0.15&#xa0;cm) showed highest similarity to stored doses. CT-calibration curve and MC-history number had a negligible influence on dose reconstruction. Dosimetric difference between reconstructed and stored doses was&#xa0;<&#xa0;1&#xa0;Gy for breast and tumour bed. Reconstructed dose was achieved&#xa0;>&#xa0;90% gamma passing rate in the validation set. However, around 2.5&#xa0;Gy dose differences were observed at the skin and tissue interface regions. CONCLUSIONS: Retrospective electron boost dose reconstruction is feasible with acceptable accuracy, and could increase data completeness in large cohort studies. Caution is advised when assessing dose near tissue interface and further validation is needed outside the REQUITE dataset.

Electrons

Harvesting backscatter electrons for radiation therapy.

PURPOSE: An innovative technique is used to harvest backscatter electrons for the treatment of superficial small lesions of skin, oral cavity, and rectum where a significant dose gradient and maximum surface dose is desired. METHODS AND MATERIALS: Backscatter electrons are harvested out of the primary electron beams from the linear accelerators. The design consists of a short cylindrical cone that fits snugly over a long cylindrical electron cone. The short cylindrical cone has a thick circular plate of high atomic number medium (Pb) attached to the distal end, and a lateral slit of variable length and width. The width of the slit could be closed as desired by rotating the two cones and the length can be increased by lowering the short cylindrical cone. Primary electrons strike the Pb plate perpendicularly and produce backscatter electrons that pass through the lateral slit for treatment. Using film and a parallel plate ion chamber, backscattered electron dose characteristics are studied. RESULTS: The depth dose characteristic of the backscatter electron is very similar to that of the 0.2 mm Al half-value layer x-ray beam that is commonly used for the intracavitary and superficial lesions. The backscatter electron energy is nearly constant and effectively < or = 1 MeV from the clinical megavoltage beams. The backscatter electron dose rate of 0.32-0.8 Gy/min could be achieved from modern accelerators without any modification. The beam flatness is dependent on the slit size and the depth of treatment, but is satisfactory to treat small lesions. CONCLUSIONS: The measured data for backscatter electron energy, fluence, depth dose, flatness, dose rate, and absolute dose indicates that the harvested backscattered electrons are suitable for clinical use.

Electrons

2-Oxo-1,2-dihydroquinoline 8-monooxygenase, a two-component enzyme system from Pseudomonas putida 86.

2-Oxo-1,2-dihydroquinoline 8-monooxygenase, which catalyzes the NADH-dependent oxygenation of 2-oxo-1,2-dihydroquinoline to 8-hydroxy-2-oxo-1,2-dihydroquinoline, is the second enzyme in the quinoline degradation pathway of Pseudomonas putida 86. This enzyme system consists of two inducible protein components, which were purified, characterized, and identified as reductase and oxygenase. The yellow reductase is a monomeric iron-sulfur flavoprotein (M(r), 38,000), containing flavin adenine dinucleotide and plant-type ferredoxin [2Fe-2S]. It transferred electrons from NADH to the oxygenase or to some artificial electron acceptors. The red-brown oxygenase (M(r), 330,000) consists of six identical subunits (M(r), 55,000) and was identified as an iron-sulfur protein, possessing about six Rieske-type [2Fe-2S] clusters and additional iron. It was reduced by NADH plus catalytic amounts of reductase. For monooxygenase activity, reductase, oxygenase, NADH, molecular oxygen, and substrate were required. The activity was considerably enhanced by the addition of polyethylene glycol and Fe2+. 2-Oxo-1,2-dihydroquinoline 8-monooxygenase revealed a high substrate specificity toward 2-oxo-1,2-dihydroquinoline, since none of 25 other tested compounds was converted. Based on its physical, chemical, and catalytic properties, we presume 2-oxo-1,2-dihydroquinoline 8-monooxygenase to belong to the class IB multicomponent non-heme iron oxygenases.

Electrons