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Powdered samples of Erianthus were treated with anhydrous ammonia at 50–140 °C. The crystal structure of cellulose in the sample changed to cellulose III I , and its crystallite size increased with increasing temperature. Lignin content decreased with increasing temperature, while most reducing sugars, including glucose, were maintained at nearly 80%. Enzymatic hydrolysis of the ammonia-treated samples was carried out at 37 °C using a mixture of cellulase and β-glucosidase in solution. The samples treated at a higher temperature showed better enzymatic degradability. Furthermore, transverse sections of Erianthus stem were also treated with ammonia, and cell wall components and their distributions were detected with microscopic observation. By using fluorescence microscopy, it was also found that lignin content decreased with increased temperature. The immuno-labeling of pectin and β-1,3-1,4-glucan showed a change to a water-soluble form and complete removal by the ammonia treatment. However, xylan had substantial resistance to ammonia treatment.

Staphylococcal alpha-hemolysin (alpha-HL) is a beta-barrel pore-forming toxin (PFT) expressed by Staphylococcus aureus. alpha-HL is secreted as a water-soluble monomeric protein, which binds to target membranes and forms membrane-inserted heptameric pores. To explore the pore-forming mechanism of alpha-HL in detail, we determined the crystal structure of the alpha-HL monomer and prepore using H35A mutant and W179A/R200A mutant, respectively. Although the overall structure of the monomer was similar to that of other staphylococcal PFTs, a marked difference was observed in the N-terminal amino latch, which bent toward the prestem. Moreover, the prestem was fastened by the cap domain with a key hydrogen bond between Asp45 and Tyr118. Prepore structure showed that the transmembrane region is roughly formed with flexibility, although the upper half of the beta-barrel is formed appropriately. Structure comparison among monomer, prepore and pore revealed a series of motions, in which the N-terminal amino latch released upon oligomerization destroys its own key hydrogen bond between Asp45 Tyr118. This action initiated the protrusion of the prestem. Y118F mutant and the N-terminal truncated mutant markedly decreased in the hemolytic activity, indicating the importance of the key hydrogen bond and the N-terminal amino latch on the pore formation. Based on these observations, we proposed a dynamic molecular mechanism of pore formation for alpha-HL.

The purpose of this study is to examine the characteristics of gait patterns in human preferred sideways locomotion at increasing speeds. Fifteen healthy young males were asked to step sideways on a treadmill at various speeds of 1.3-6.1 km/h. The times of foot contact and take-off were analyzed. Three gait patterns were observed. At slow speeds, all of the subjects performed a walk-like pattern. When the treadmill speed exceeded approximately 3.5 km/h, the subjects preferred gait patterns with a flight phase. Most of the subjects performed an asymmetric gait pattern that was similar to a forward gallop, whereas only two out of fifteen subjects performed a run-like gait pattern. Because the left and right legs are positioned along the movement direction, it might be more efficient to divide roles between the leading and trailing limbs at high speeds: the leading limb functions to produces breaking and vertical force, and the trailing limb mainly absorbs the impact of foot contact and generates propulsive forces.