A 30-year-old man presented with pain and limitation of movement of the right hip. The symptoms had failed to respond to conservative treatment. Radiographs and CT scans revealed evidence of impingement between the femoral head-neck junction and an abnormally large anterior inferior iliac spine. Resection of the hypertrophic anterior inferior iliac spine was performed which produced full painless restoration of function of the hip. Hypertrophy of the anterior inferior iliac spine as a cause of femoro-acetabular impingement has not previously been described.

The purpose of this work is to reveal the effects of the energetic particle mode (EPM) on fast-ion transport and consequent fast-ion loss in the compact helical system (CHS). For this purpose, fast particle diagnostics capable of following fast events originating from the EPM (f < 100 kHz) and from the toroidicity-induced Alfvén eigenmode (TAE) (f = 100-200 kHz) are employed in CHS. Experiments show that the EPM excited by co-circulating fast ions in an outward-shifted configuration is identified as a mode of m/n = 3/2 and can enhance fast-ion loss when its magnetic fluctuation amplitude exceeds ∼4 × 10 −5 T at the magnetic probe position. The lost fast-ion probe (LIP) located at the outboard side of the torus indicates that bursting EPMs lead to periodically enhanced losses of co-going fast ions having smaller pitch angles in addition to losses of marginally co-passing fast ions. Coinciding with EPM bursts, the Hα light detector viewing the peripheral region at the outboard side also shows large pulsed increases similar to that of the LIP whereas the detector viewing the peripheral region at the inboard side does not. This is also evidence that fast ions are expelled to the outboard side due to the EPM. The charge-exchange neutral particle analyser indicates that only fast ions whose energy is close to the beam injection energy E b are strongly affected by EPM, suggesting in turn that observed EPMs are excited by fast ions having energy close to E b .

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Two free flavin-independent enzymes were purified by detecting the NAD(P)H oxidation in the presence of Fe(III)-EDTA and t-butyl hydroperoxide from E. coli. The enzyme that requires NADH or NADPH as an electron donor was a 28 kDa protein, and N-terminal sequencing revealed it to be oxygen-insensitive nitroreductase (NfnB). The second enzyme that requires NADPH as an electron donor was a 30 kDa protein, and N-terminal sequencing revealed it to be ferredoxin-NADP(+) reductase (Fpr). The chemical stoichiometry of the Fenton activities of both NfnB and Fpr in the presence of Fe(III)-EDTA, NAD(P)H and hydrogen peroxide was investigated. Both enzymes showed a one-electron reduction in the reaction forming hydroxyl radical from hydrogen peroxide. Also, the observed Fenton activities of both enzymes in the presence of synthetic chelate iron compounds were higher than their activities in the presence of natural chelate iron compounds. When the Fenton reaction occurs, the ferric iron must be reduced to ferrous iron. The ferric reductase activities of both NfnB and Fpr occurred with synthetic chelate iron compounds. Unlike NfnB, Fpr also showed the ferric reductase activity on an iron storage protein, ferritin, and various natural iron chelate compounds including siderophore. The Fenton and ferric reductase reactions of both NfnB and Fpr occurred in the absence of free flavin. Although the k(cat)/K(m) value of NfnB for Fe(III)-EDTA was not affected by free flavin, the k(cat)/K(m) value of Fpr for Fe(III)-EDTA was 12-times greater in the presence of free FAD than in the absence of free FAD.

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