Measurement of the response-ratio of an ionization chamber filled with dry air to that filled with P-10 gas in the calibration of gas monitors.
We developed a new method to determine the response ratio of an ionization chamber (Ohkura ionization chamber: type I-4096 01/06) filled with dry air to that filled with P-10 gas. The response-ratio was obtained by comparing the output currents of the ionization chamber after introduction of radioactive gasses of identical activities contained in two small vessels. The obtained ratio was 0.690 ± 0.003, which agreed with the results obtained by other methods.
Activity measurement of 85Kr diluted by a large volume balloon technique.
The National Metrology Institute of Japan (NMIJ) participated in the CCRI(II) Key-comparison of (85)Kr activity measurement. The absolute internal gas-counting method was used, with a set of proportional counters of different length. The original (85)Kr gas was diluted by a factor of 2x10(5) in order to achieve the suitable activity concentration for the proportional counters. A new dilution method was introduced, based on a large-volume balloon and gravimetric determination of the dilution volume with small uncertainties.
Molecular diversity of skin mucus lectins in fish.
Among lectins in the skin mucus of fish, primary structures of four different types of lectin have been determined. Congerin from the conger eel Conger myriaster and AJL-1 from the Japanese eel Anguilla japonica were identified as galectin, characterized by its specific binding to beta-galactoside. Eel has additionally a unique lectin, AJL-2, which has a highly conserved sequence of C-type lectins but displays Ca(2+)-independent activity. This is rational because the lectin exerts its function on the cutaneous surface, which is exposed to a Ca(2+) scarce environment when the eel is in fresh water. The third type lectin is pufflectin, a mannose specific lectin in the skin mucus of pufferfish Takifugu rubripes. This lectin showed no sequence similarity with any known animal lectins but, surprisingly, shares sequence homology with mannose-binding lectins of monocotyledonous plants. The fourth lectin was found in the ponyfish Leiognathus nuchalis and exhibits homology with rhamnose-binding lectins known in eggs of some fish species. These lectins, except ponyfish lectin, showed agglutination of certain bacteria. In addition, pufflectin was found to bind to a parasitic trematode, Heterobothrium okamotoi. Taken together, these results demonstrate that skin mucus lectins in fish have wide molecular diversity.