138 resultados para GOAL-DIRECTED MOVEMENTS
Resumo:
Understanding how the timing of motor output is coupled to sensory temporal information is largely based on synchronisation of movements through small motion gaps (finger taps) to mostly empty sensory intervals (discrete beats). This study investigated synchronisation of movements between target barriers over larger motion gaps when closing time gaps of intervals were presented as either continuous, dynamic sounds, or discrete beats. Results showed that although synchronisation errors were smaller for discrete sounds, the variability of errors was lower for continuous sounds. Furthermore, finger movement between targets was found to be more sinusoidal when continuous sensory information was presented during intervals compared to discrete. When movements were made over larger amplitudes, synchronisation errors tended to be more positive and movements between barriers more sinusoidal, than for movements over shorter amplitudes. These results show that the temporal control of movement is not independent from the form of the sensory information that specifies time gaps or the magnitude of the movement required for synchronisation.
Resumo:
The excreted/secreted proteinases of adult and juvenile Fasciola hepatica maintained in vitro were found to hydrolyse the fluorogenic substrates Cbz-Phe-Arg- and Cbz-Arg-Arg-NHMec. This activity was demonstrated to have a classical cysteine proteinase inhibitor profile, with turn-over of both substrates being blocked by pre-incubation with E64 and peptidyl diazomethanes. The Cbz-Arg-Arg-NHMec hydrolysing activity of the mature fluke exhibited an alkaline stability not characteristic of its mammalian lysosomal counterparts. Further, the biotinylated affinity reagents biotin-Phe-Ala CHN2 and biotin-Phe-Cys(SBzyl)-CHN2 were used to label and characterize these cysteine proteinases in terms of apparent molecular weight and subsite specificity. Adult fluke media were found to contain four species of molecular weights 66, 58, 50 and 25-26 kDa; juvenile media contained three species of molecular weights 66, 54 and 25-26 kDa. The major 25-26 kDa cysteine proteinase common to both stages was shown to have a subsite specificity similar to that of mammalian cathepsin B.