Membrane transport of long-chain fatty acids: evidence for a facilitated process

In mammalian cells, membrane uptake of long-chain fatty acids is mediated by two separate components; a passive component that is a linear function of the concentration of free fatty acid in the extracellular medium and a saturable component that exhibits the characteristics of a protein-facilitated process. This review summarizes the body of work that has accumulated related to the mechanism of fatty acid transport. Evidence in support of a facilitated uptake process is presented with relation to the different cell types or membrane systems where it was collected. The evidence includes saturation kinetics, competition between different substrates, and sensitivity to a variety of inhibitors. Recent knowledge related to membrane proteins thought to be implicated in the uptake process is reviewed. Factors that may modulate uptake or alter the relative contribution of passive versus facilitated components are briefly discussed. These include the molar ratio of fatty acid to its physiological carrier, plasma albumin and the metabolic or hormonal milieu.     

Buffer Standards for the Biological pH of the Amino Acid N-[2 hydroxyethyl]piperazine-N'-[3-propanesulfonic acid], HEPPS, From (278.15 to 328.15) K

For the HEPPS buffer under investigation, there are seven buffer solutions without NaCl and eight buffer solutions that contain Cl(-) and have an ionic strength (I = 0.16 mol·kg(-1)), which is similar to that of blood plasma. These buffer solutions have been evaluated in the temperature range of (278.15 to 328.15) K using the extended Debye- Hückel equation and the Bates-Guggenheim convention. The previously determined E(j) values have been used to determine the operational pH values of HEPPS buffer solutions at (298.15 and 310.15) K. These are recommended as secondary standard reference solutions for pH measurements in saline media with an isotonic ionic strength of I = 0.16 mol·kg(-1).     

Glucocorticoid receptor binding to rat liver nuclei occurs without nuclear transport

The binding of cell-free activated glucocorticoid receptor-steroid complexes from HTC cells to various preparations of HTC and rat liver nuclei has been examined under conditions that did or did not support the nuclear translocation of macromolecules via nuclear pores. To the best of our knowledge, this is the first such study with functionally active isolated nuclei. Conventionally prepared HTC nuclei were found to be porous, as determined from their inability to exclude the fluorescent macromolecule phycoerythrin (PE) at 4 degrees C. Thus the nuclear binding of activated complexes to these nuclei can not involve nuclear translocation. Further studies, using established conditions with sealed nuclei prepared from rat liver, revealed that nuclear translocation of PE containing a covalently linked, authentic nuclear translocation sequence could be obtained at 22 degrees C, but not at 4 degrees C. However, under the same conditions, activated glucocorticoid complexes displayed equal levels of nuclear binding at both temperatures. We therefore conclude that the current translocation conditions with intact rat liver nuclei are not sufficient to reproduce the nuclear transport of glucocorticoid complexes observed in intact cells. The nuclear binding that was seen with intact rat liver nuclei was not affected by aurintricarboxylic acid, which selectively inhibits protein-nucleic acid interactions. The antibody AP-64, shown to be specific for amino acids 506-514 of the nuclear translocation sequence of the rat glucocorticoid receptor, inhibited the nuclear binding of activated complexes, apparently by blocking receptor access to the nuclear membrane. Collectively, these data argue that activated complex binding to nuclei capable of nuclear translocation involves only an association with nuclear membrane components such as nuclear pores. Thus this system, and these reagents, may be useful in future studies of activated complex binding to nuclear pores.     

Planar MESFET transmission wave amplifier

The authors present a quasioptical power combining transmission amplifier for increasing the power level available from solid-state circuits. Receiving and transmitting arrays of patch antennas, input/output isolation, MESFETs, bias and matching circuitry are contained on a single substrate, making monolithic millimetre-wave integration possible. The flexibility of selecting input polarisation with respect to the output while maintaining amplifier stability is demonstrated. A 24-MESFET patch antenna amplifier array is presented.<>     

Thermal stability of the nickel-base superalloy B-1900 + Hf with tantalum variations

The microstructure of the solutionized and aged nickel-base superalloy B-1900 + Hf was examined after additional aging at 982 °C for 72, 250, and 1000 hours. Alloy compositions that were examined contained the normal 1.34 at. pct (4.3 wt pct). Ta as well as 0.67 at. pct and zero Ta levels. The γ phase agglomerated, became plate-like in morphology, and decreased in volume fraction for all three alloys throughout the aging treatments. Changes which occurred in the γ and γ' phase compositions were nearly complete after 72 hours of aging while changes in the MC carbide composition continued throughout the aging. Blocky M₆C carbides precipitated along the grain boundaries of all three alloys in the first 72 hours of aging. In addition, an acicular form of this Mo/Cr/Ni-rich carbide developed in the intragranular regions of the Ta-containing alloys. Formerly an Undergraduate Student, Department of Metallurgical Engineering, Michigan Technological University.