The neutral beam (NB) fast ion confinement in the Large Helical Device (LHD) is studied for several full field ( $B_{t}\sim 2.75~\text{T}$ ) magnetic configurations by a combination of neutron measurement and simulations. To investigate the NB fast ion confinement, we have performed a series of short-pulse NB injection experiments. The experiment results are analysed by the integrated code TASK3D-a. From this investigation, the effective particle diffusion coefficients of the tangential and perpendicular NBs are approximately $D^{\text{eff}}\sim 0.1~\text{m}^{2}~\text{s}^{-1}$ and $D^{\text{eff}}\sim 1~\text{m}^{2}~\text{s}^{-1}$ in the standard configuration. It is clarified that the NB fast ion confinement improves when the plasmas are shifted inward. Moreover, it is also found that the simulation, which considers the deuteron dilution effect due to the presence of impurity ions, can describe a neutron emission rate consistent with the measurement.

A structure called ‘veil’ in Theileria sergenti-, T. buffeli- or T. orientalis-infected bovine erythrocytes was purified from erythrocyte lysates by Percoll density-gradient centrifugation. On electron microscopical examination, the veils consisted of electron-dense material showing a periodicity of striations and were not surrounded by membranes. Analyses of veil proteins by one- and two-dimensional polyacrylamide gel electrophoresis revealed that the veils contain haemoglobin and several other basic proteins of molecular weight ranging from 15·5 to 46 kDa. By comparing the protein patterns of the veil with those of purified piroplasms and uninfected bovine erythrocytes, these basic proteins appeared to be of parasite origin. It would appear likely that the veils formed by intra-erythrocytic precipitation of haemoglobin and proteins excreted by the parasites. Differences in veil constituents were found between T. sergenti, T. buffeli and T. orientalis.

Proteins of the piroplasms of Theileria sergenti, T. buffeli and T. orientalis were analysed by two-dimensional polyacrylamide gel electrophoresis. Protein spot patterns of T. buffeli and T. orientalis were identical except for a few minor proteins, whereas spot patterns of two T. sergenti stocks were differentiated from those of T. buffeli and T. orientalis by a characteristic set of proteins including a major protein of molecular weight 33–34 kDa. This result indicates that Japanese T. sergenti can be phenotypically distinguishable from European and Australia Theileria species; T. orientalis and T. buffeli.