Fates and Travel Times of Denmark Strait Overflow Water in the Irminger Basin*

The Denmark Strait Overflow (DSO) supplies about one-third of the North Atlantic Deep Water and is critical to global thermohaline circulation. Knowledge of the pathways of DSO through the Irminger Basin and its transformation there is still incomplete, however. The authors deploy over 10 000 Lagrangian particles at the Denmark Strait in a high-resolution ocean model to study these issues. First, the particle trajectories show that the mean position and potential density of dense waters cascading over the Denmark Strait sill evolve consistently with hydrographic observations. These sill particles transit the Irminger Basin to the Spill Jet section (65.25°N) in 5–7 days and to the Angmagssalik section (63.5°N) in 2–3 weeks. Second, the dense water pathways on the continental shelf are consistent with observations and particles released on the shelf in the strait constitute a significant fraction of the dense water particles recorded at the Angmagssalik section within 60 days (~25%). Some particles circulate on the shelf for several weeks before they spill off the shelf break and join the overflow from the sill. Third, there are two places where the water density following particle trajectories decreases rapidly due to intense mixing: to the southwest of the sill and southwest of the Kangerdlugssuaq Trough on the continental slope. After transformation in these places, the overflow particles exhibit a wide range of densities

Purification and properties of inosine-guanosine phosphorylase from Escherichia coli K-12.

A xanthosine-inducible enzyme, inosine-guanosine phosphorylase, has been partially purified from a strain of Escherichia coli K-12 lacking the deo-encoded purine nucleoside phosphorylase. Inosine-guanosine phosphorylase had a particle weight of 180 kilodaltons and was rapidly inactivated by p-chloromercuriphenylsulfonic acid (p-CMB). The enzyme was not protected from inactivation by inosine (Ino), 2'-deoxyinosine (dIno), hypoxanthine (Hyp), Pi, or alpha-D-ribose-1-phosphate (Rib-1-P). Incubating the inactive enzyme with dithiothreitol restored the catalytic activity. Reaction with p-CMB did not affect the particle weight. Inosine-guanosine phosphorylase was more sensitive to thermal inactivation than purine nucleoside phosphorylase. The half-life determined at 45 degrees C between pH 5 and 8 was 5 to 9 min. Phosphate (20 mM) stabilized the enzyme to thermal inactivation, while Ino (1 mM), dIno (1 mM), xanthosine (Xao) (1 mM), Rib-1-P (2 mM), or Hyp (0.05 mM) had no effect. However, Hyp at 1 mM did stabilize the enzyme. In addition, the combination of Pi (20 mM) and Hyp (0.05 mM) stabilized this enzyme to a greater extent than did Pi alone. Apparent activation energies of 11.5 kcal/mol and 7.9 kcal/mol were determined in the phosphorolytic and synthetic direction, respectively. The pH dependence of Ino cleavage or synthesis did not vary between 6 and 8. The substrate specificity, listed in decreasing order of efficiency (V/Km), was: 2'-deoxyguanosine, dIno, guanosine, Xao, Ino, 5'-dIno, and 2',3'-dideoxyinosine. Inosine-guanosine phosphorylase differed from the deo operon-encoded purine nucleoside phosphorylase in that neither adenosine, 2'-deoxyadenosine, nor hypoxanthine arabinoside were substrates or potent inhibitors. Moreover, the E. coli inosine-guanosine phosphorylase was antigenically distinct from the purine nucleoside phosphorylase since it did not react with any of 14 monoclonal antisera or a polyvalent antiserum raised against deo-encoded purine nucleoside phosphorylase