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I Schall

Publications and source records attributed to I Schall.

5 recordsLinked to original sources

Nuclear fragmentation of high-energy heavy-ion beams in water.

As a part of the physical-technical program of the heavy-ion therapy project at GSI we have investigated the nuclear fragmentation of high-energy ion beams delivered by the heavy-ion synchrotron SIS, using water as a tissue-equivalent target. For a direct comparison of fragmentation properties, beams of 10B, 12C, 14N, and 16O were produced simultaneously as secondary beams from a primary 18O beam and separated in flight by magnetic beam analysis. The Z-distributions of beam fragments produced in the water target were measured via energy loss in a large ionisation chamber and a scintillator telescope. From these data we obtained both total and partial charge-changing cross sections. In addition we have performed Bragg measurements using two parallel-plate ionization chambers and a water target of variable length. The detailed shape of the measured Bragg curves and the measured cross sections are in good agreement with model calculations based on semi-empirical formulae.

Boron↗

Neonatal and adult patterns of lectin binding to rat small intestinal microvillus membranes.

To investigate postnatal developmental changes of rat small intestinal microvillus membrane (MVM) sugar components, binding studies were done using peanut agglutinin (PNA) and soybean agglutinin (SBA). MVM were prepared from rats of different ages (new-borns to 12 weeks). The Airfuge method was used for separation of unbound material. Characteristics of sugar ligand specificity were different for PNA and SBA, although D(+)galactose was used as an inhibitor for both lectins. Concentration curves and Scatchard plots showed partial saturation of total binding, and at least two groups of MVM ligands. Differences in lectin binding between newborn and adult MVM were opposite for PNA and SBA (newborns bound more PNA, but less SBA). During the first few postnatal weeks in rats, SBA binding changed early, and PNA binding exhibited an intermediate change, not related to weaning. Changes in MVM glycoproteins shown by lectin binding appear to be part of a complex postnatal maturational process in rats, involving different biochemical, functional, and biophysical membrane characteristics.

Analysis of Variance↗