PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 11542671

Nuclear absorption cross sections using medium modified nucleon-nucleon amplitudes.

R K Tripathi·J W Wilson·F A Cucinotta
View original source ↗Export metadata ↓

Abstract

We extract the in-medium nucleon-nucleon amplitudes from the available proton-nucleus total reaction cross sections data. The retrieval of the information from the experiment makes these estimates very reliable. Simple expressions are then given for the in-medium nucleon-nucleon amplitudes for any system of colliding nuclei as a function of energy. Excellent agreement is demonstrated in ion-nucleus absorption cross sections.

Explore related subjects

AluminumCarbonElementary ParticlesEnergy TransferIronLeadModels, TheoreticalNuclear PhysicsProtonsReproducibility of ResultsScattering, RadiationNASA Discipline Radiation HealthJournal ArticleResearch Support, U.S. Gov't, Non-P.H.S.

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

R K Tripathi, J W Wilson, F A Cucinotta. 1998. Nuclear absorption cross sections using medium modified nucleon-nucleon amplitudes.. https://doi.org/10.1016/s0168-583x(98)00420-0

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

KEEP EXPLORING

Related citations

PubMed2003

Effects of temperature on the recovery of juvenile grayling (Thymallus thymallus) from exposure to Al+Fe.

One-summer-old graylings (Thymallus thymallus) were exposed for 6 days to water containing a mixture of 1 mg l(-1) Fe and 100 microg l(-1) Al at pH 5.5, with or without 15 mg l(-1) humic acid. A pH of 6.9 was used as a control. The experiment was performed at two test temperatures, 13 and 3 degrees C. After 1 week of exposure, half of the fish in the tank were taken for oxygen measurement and tissue sampling. The remaining half were maintained in metal-free water for a further week to assess their recovery at the two test temperatures. Fifty percent of the fish died under metal exposure at 13 degrees C, but none at 3 degrees C. Despite of the lack of mortalities at the lower temperature, surviving fish at both test temperatures suffered similar gill damage (adherence of lamellae), disturbances in ion regulation, increases in haematocrit value (Hct) and haemoglobin (Hb) concentration and reductions in oxygen consumption. The addition of humic acid prevented these changes. The reduced plasma chloride concentration, increased blood Hct value and Hb concentration recovered completely at 13 degrees C, whereas the lowered oxygen consumption recovered less completely, which may be attributed to the remaining minor gill damage (lamellar hypertrophy). At the lower temperature, the adherence of lamellae persisted after the recovery period, and oxygen consumption, therefore, remained at a very low level. The decreased plasma chloride concentration was also unable to recover. The accumulation of Al inside the gill tissue was greater at low temperature. We conclude that the acute toxicity of a mixture of Fe and Al to grayling and their subsequent ability to recovery is dependent on the exposure temperature.

Aluminum↗
PubMed2003

Measurements of contact potential difference (work functions) of metals and semiconductors surface by the static ionized capacitor method.

Electron work functions of several metals (Au, W, Ag, Cu, Mo, Ti, Al) and Si at atmospheric conditions have been measured by the method of the static capacitor with an ionized gap between the electrodes. Results for all samples, excluding Au, Al and Si, conform to reference data with an accuracy of +/- 1.0%. For samples Au, Al and Si, the electron work function values conform to reference data after short-time heat treatment at atmospheric conditions at 200 degrees C (for Al) and 600 degrees C (for Au, Si).

Aluminum↗
PubMed2003

Binding studies on aluminum(III)-albumin interaction.

The present paper reports a quantitative investigation on the binding of aluminum to human serum albumin. Equilibrium dialysis and a general thermodynamic approach have been used to determine the binding parameters. Two aluminum binding sites have been identified on the albumin molecule, involving sites with single and double occupancy modes. The binding properties of these two distinct sites appear to undergo reciprocal influences, suggesting a possible interaction between the corresponding protein moieties. Both coordination modes proceed from weak interactions, as shown by the binding energies calculated.

Aluminum↗