STUDIES ON THE EXPLOSION (PART 1) : ON THE PRILLED AMMONIUM NITRATE

We observed prilled ammonium nitrate by the electron and optical microscopes. Wealso measured its bulk density, ratio of oil absorption and the detonation velocity of ~mmoniumnitrate fuel oil blasting agents, I. E. the mixture of the prilled AN and FO. We further madethe cap sensitivity tests and the drop hammer tests.Through these measurings and testings, we concluded that the prilled AN which had thefollowing properties was the most suitable for ANFO blasting agents; bulk density: 0.75 .-0.85g/cc, ratio of oil absorption: IO-2Og/ 100 g AN, water content: 0.5% or below, detonationvelocity: 2, 500-3, 300m 'sec, cap sensitivity: unable to be detonated by a No.8 cap.We observed prilled ammonium nitrate by the electron and optical microscopes. Wealso measured its bulk density, ratio of oil absorption and the detonation velocity of ~mmoniumnitrate fuel oil blasting agents, I. E. the mixture of the prilled AN and FO. We further madethe cap sensitivity tests and the drop hammer tests.Through these measurings and testings, we concluded that the prilled AN which had thefollowing properties was the most suitable for ANFO blasting agents; bulk density: 0.75 .-0.85g/cc, ratio of oil absorption: IO-2Og/ 100 g AN, water content: 0.5% or below, detonationvelocity: 2,500-3,300m 'sec, cap sensitivity: unable to be detonated by a No.8 cap

Miro1 Is a Calcium Sensor for Glutamate Receptor-Dependent Localization of Mitochondria at Synapses

Energy use, mainly to reverse ion movements in neurons, is a fundamental constraint on brain information processing. Trafficking of mitochondria to locations in neurons where there are large ion fluxes is essential for powering neural function. Mitochondrial trafficking is regulated by Ca2+ entry through ionotropic glutamate receptors, but the underlying mechanism is unknown. We show that the protein Miro1 links mitochondria to KIF5 motor proteins, allowing mitochondria to move along microtubules. This linkage is inhibited by micromolar levels of Ca2+ binding to Miro1. With the EF hand domains of Miro1 mutated to prevent Ca2+ binding, Miro1 could still facilitate mitochondrial motility, but mitochondrial stopping induced by glutamate or neuronal activity was blocked. Activating neuronal NMDA receptors with exogenous or synaptically released glutamate led to Miro1 positioning mitochondria at the postsynaptic side of synapses. Thus, Miro1 is a key determinant of how energy supply is matched to energy usage in neurons