Passive propellant system

The system utilizes a spherical tank structure A separated into two equal volume compartments by a flat bulkhead B. Each compartment has four similar gallery channel legs located in the principal vehicle axes, ensuring that bulk propellant will contact at least one gallery leg during vehicle maneuvers. The forward compartment gallery channel legs collect propellant and feed it into the aft compartment through communication screens which protrude into the aft compartment. The propellant is then collected by the screened gallery channels in the aft compartment and supplied to the propellant outlet. The invention resides in the independent gallery assembly and screen structure by means of which propellant flow from forward to aft compartments is maintained. Liquid surface tension of the liquid on the screens is used to control liquid flow. The system provides gas-free propellants in low or zero-g environments regardless of axial accelerations and propellant orientation in bulk regions of the vessel

An Isotopic analysis of the hydrology and riparian vegetation water sources on Bishop Creek

Five power generation plants along an eleven kilometer stretch divert Bishop Creek water for hydro-electric power. Stream diversion may be adversely affecting the riparian vegetation. Stable isotopic analysis is employed to determine surface water/ground-water interactions along the creek. surface water originates primarily from three headwater lakes. Discharge into Bishop Creek below the headwaters is primarily derived from ground water. The average δD and δ18O values are significantly different for surface water and ground water that an isotopic analysis can delineate between these two components of flow. Therefore isotopic shifts along the creek can determine gaining reaches. In addition, by knowing the isotopic signatures of various waters in the watershed, it may be possible to examine tree waters to determine their water source(s)

Jupiter's radiation belts: Can Pioneer 10 survive?

Model calculations of Jupiter's electron and proton radiation belts indicate that the Galilean satellites can reduce particle fluxes in certain regions of the inner magnetosphere by as much as six orders of magnitude. Average fluxes should be reduced by a factor of 100 or more along the Pioneer 10 trajectory through the heart of Jupiter's radiation belts in early December. This may be enough to prevent serious radiation damage to the spacecraft

Calculation of compressible flow about three-dimensional inlets with auxiliary inlets, slats and vanes by means of a panel method

An efficient and user oriented method was constructed for calculating flow in and about complex inlet configurations. Efficiency is attained by: (1) the use of a panel method; (2) a technique of superposition for obtaining solutions at any inlet operating condition; and (3) employment of an advanced matrix iteration technique for solving large full systems of equations, including the nonlinear equations for the Kutta condition. User concerns are addressed by the provision of several novel graphical output options that yield a more complete comprehension of the flowfield than was possible previously

Absorption of trapped particles by Jupiter's moons

Absorption effects of the four innermost moons in the radial transport equations for electrons and protons in Jupiter's magnetosphere are presented. The phase space density n at 2 R sub J for electrons with equatorial pitch angles less than 69 deg is reduced by a factor of 4.2 x 1000 when lunar absorption is included in the calculation. For protons with equatorial pitch angles less than 69 deg, the corresponding reduction factor is 3.2 x 100000. The effect of the satellites becomes progressively weaker for both electrons and protons as equatorial pitch angles of pi/2 are approached, because the likelihood of impacting a satellite becomes progressively smaller. The large density decreases which we find at the orbits of Io, Europa, and Ganymede result in corresponding particle flux decreases that should be observed by spacecraft making particle measurements in Jupiter's magnetosphere. The characteristic signature of satellite absorption should be a downward pointing cusp in the flux versus radius curve at the L-value corresponding to each satellite

Glucocorticoid-regulated localization of cell surface glycoproteins in rat hepatoma cells is mediated within the Golgi complex.

Glucocorticoid hormones regulate the post-translational maturation and sorting of cell surface and extracellular mouse mammary tumor virus (MMTV) glycoproteins in M1.54 cells, a stably infected rat hepatoma cell line. Exposure to monensin significantly reduced the proteolytic maturation and externalization of viral glycoproteins resulting in a stable cellular accumulation of a single 70,000-Mr glycosylated polyprotein (designated gp70). Cell surface- and intracellular-specific immunoprecipitations of monensin-treated cells revealed that gp70 can be localized to the cell surface only in the presence of 1 microM dexamethasone, while in uninduced cells gp70 is irreversibly sequestered in an intracellular compartment. Analysis of oligosaccharide processing kinetics demonstrated that gp70 acquired resistance to endoglycosidase H with a half-time of 65 min in the presence or absence of hormone. In contrast, gp70 was inefficiently galactosylated after a 60-min lag in uninduced cells while rapidly acquiring this carbohydrate modification in the presence of dexamethasone. Furthermore, in the absence or presence of monensin, MMTV glycoproteins failed to be galactosylated in hormone-induced CR4 cells, a complement-selected sorting variant defective in the glucocorticoid-regulated compartmentalization of viral glycoproteins to the cell surface. Since dexamethasone had no apparent global effects on organelle morphology or production of total cell surface-galactosylated species, we conclude that glucocorticoids induce the localization of cell surface MMTV glycoproteins by regulating a highly selective step within the Golgi apparatus after the acquisition of endoglycosidase H-resistant oligosaccharide side chains but before or at the site of galactose attachment