47 research outputs found
The Devon Island Expedition
In 1959 the Arctic Institute of North America undertook an integrated program of long term research on Devon Island in the Queen Elizabeth Islands of arctic Canada. The co-ordinated studies were designed to help understand the interrelationships between the glacier ice of Devon Island, the ocean in Jones Sound, and the encompassing atmosphere. They are being carried out over a 3-year period under the leadership of Spencer Apollonio. The main effort is concentrated on attempts to evaluate such factors as physical, chemical, and biological variations in the arctic waters of Jones Sound caused by discharging glaciers; evaporation and transfer of moisture between the ocean waters and the ice-cap and glaciers; and the overall influences of solar radiation energy on the mass balance of the ice-cap, the biological production in the sea, and the growth and decay of sea-ice. Some supplementary studies in archaeology and geology are included in the expedition's work because of the marked deficiency of knowledge in those subjects for Devon Island. In the late summer of 1960 a main base was established on the north shore of Devon Island near Cape Skogn by an advance party of eight men taken in with their materials by the Canada Department of Transport icebreaker "d'Iberville". During a 3-week period buildings were erected and routes inland and to the ice-cap explored and marked, while an archaeological reconnaissance of the Cape Sparbo area was made by a small party under Mr. Gordon Lowther of McGill University. Everything was installed for a beginning of the 3-year program in April 1961. During the months of April to September 1961 21 men worked on extensive programs in geophysics, glaciology, marine biology and oceanography, meteorology, and surveying. Intensive work was also completed in archaeology and geology. ..
Independent Ion Migration in Suspensions of Strongly Interacting Charged Colloidal Spheres
We report on sytematic measurements of the low frequency conductivity in
aequous supensions of highly charged colloidal spheres. System preparation in a
closed tubing system results in precisely controlled number densities between
1E16/m3 and 1E19/m^3 (packing fractions between 1E-7 and 1E-2) and electrolyte
concentrations between 1E-7 and 1E-3 mol/l. Due to long ranged Coulomb
repulsion some of the systems show a pronounced fluid or crystalline order.
Under deionized conditions we find s to depend linearily on the packing
fraction with no detectable influence of the phase transitions. Further at
constant packing fraction s increases sublinearily with increasing number of
dissociable surface groups N. As a function of c the conductivity shows
pronounced differences depending on the kind of electrolyte used. We propose a
simple yet powerful model based on independent migration of all species present
and additivity of the respective conductivity contributions. It takes account
of small ion macro-ion interactions in terms of an effectivly transported
charge. The model successfully describes our qualitatively complex experimental
observations. It further facilitates quantitative estimates of conductivity
over a wide range of particle and experimental parameters.Comment: 32 pages, 17 figures, 2 tables, Accepted by Physical Review
Expression of Actin-interacting Protein 1 Suppresses Impaired Chemotaxis of Dictyostelium Cells Lacking the Na+-H+ Exchanger NHE1
Dictyostelium cells lacking the intracellular pH regulator NHE1 have defective chemotaxis. A modifier screen and reconstitution studies show expression of recombinant actin interacting protein 1 (Aip1) suppresses the Ddnhe1-phenotype. Aip1 promotes cofilin-dependent actin remodeling, which is likely a major determinant in pH-dependent chemotaxis
Structural and kinetic studies of induced fit in xylulose kinase from Escherichia coli
The primary metabolic route for D-xylose, the second most abundant sugar in nature, is via the pentose phosphate pathway after a two-step or three-step conversion to xylulose-5-phosphate. Xylulose kinase (XK; EC 2.7.1.17) phosphorylates D-xylulose, the last step in this conversion. The apo and D-xylulose-bound crystal structures of Escherichia coli XK have been determined and show a dimer composed of two domains separated by an open cleft. XK dimerization was observed directly by a cryo-EM reconstruction at 36 A resolution. Kinetic studies reveal that XK has a weak substrate-independent MgATP-hydrolyzing activity, and phosphorylates several sugars and polyols with low catalytic efficiency. Binding of pentulose and MgATP to form the reactive ternary complex is strongly synergistic. Although the steady-state kinetic mechanism of XK is formally random, a path is preferred in which D-xylulose binds before MgATP. Modelling of MgATP binding to XK and the accompanying conformational change suggests that sugar binding is accompanied by a dramatic hinge-bending movement that enhances interactions with MgATP, explaining the observed synergism. A catalytic mechanism is proposed and supported by relevant site-directed mutants
The PPP-Family Protein Phosphatases PrpA and PrpB of Salmonella enterica Serovar Typhimurium Possess Distinct Biochemical Properties
Salmonella enterica serovar Typhimurium requires Mn(2+), but only a few Mn(2+)-dependent enzymes have been identified from bacteria. To characterize Mn(2+)-dependent enzymes from serovar Typhimurium, two putative PPP-family protein phosphatase genes were cloned from serovar Typhimurium and named prpA and prpB. Their DNA-derived amino acid sequences showed 61% identity to the corresponding Escherichia coli proteins and 41% identity to each other. Each phosphatase was expressed in E. coli and purified to near electrophoretic homogeneity. Both PrpA and PrpB absolutely required a divalent metal for activity. As with other phosphatases of this class, Mn(2+) had the highest affinity and stimulated the greatest activity. The apparent K(a) of PrpA for Mn(2+) of 65 Ī¼M was comparable to that for other bacterial phosphatases, but PrpB had a much higher affinity for Mn(2+) (1.3 Ī¼M). The pH optima were pH 6.5 for PrpA and pH 8 for PrpB, while the optimal temperatures were 45 to 55Ā°C for PrpA and 30 to 37Ā°C for PrpB. Each phosphatase could hydrolyze phosphorylated serine, threonine, or tyrosine residues, but their relative specific activities varied with the specific substrate tested. These differences suggest that each phosphatase is used by serovar Typhimurium under different growth or environmental conditions such as temperature or acidity