Textbook of Adult Emergency Medicine

Now fully revised and updated, Textbook of Adult Emergency Medicine provides clear and consistent coverage of this rapidly evolving specialty. Building on the success of previous editions, it covers all the major topics that present to the trainee doctor in the emergency department. It will also prove invaluable to the range of other professionals working in this setting - including nurse specialists and paramedics - who require concise, highly practical guidance, incorporating latest best practice and current guidelines. For the first time this edition now comes with a complete and enhanced electronic version, providing a richer learning experience and making rapid reference easier than ever before, anytime, anywhere

Ex-situ Bioremediation of U(VI) from Contaminated Mine Water Using Acidithiobacillus ferrooxidans Strains

The ex-situ bioremoval of U(VI) from contaminated water using Acidithiobacillus ferrooxidans strain 8455 and 13538 was studied under a range of pH and uranium concentrations. The effect of pH on the growth of bacteria was evaluated across the range 1.5–4.5 pH units. The respiration rate of At. ferrooxidans at different U(VI) concentrations was quantified as a measure of the rate of metabolic activity over time using an oxygen electrode. The biosorption process was quantified using a uranyl nitrate solution, U-spiked growth media, and U-contaminated mine water. The results showed that both strains of At. ferrooxidans are able to remove U(VI) from solution at pH 2.5–4.5, exhibiting a buffering capacity at pH 3.5. The respiration rate of the micro-organism was affected at U(VI) concentration of 30 mg L−1. The kinetics of the sorption fitted a pseudo-first order equation, and depended on the concentration of U(VI). The KD obtained from the biosorption experiments indicated that strain 8455 is more efficient for the removal of U(VI). A bioreactor designed to treat a solution of 100 mg U(VI) L−1 removed at least 50% of the U(VI) in water. The study demonstrated that At. ferrooxidans can be used for the ex-situ bioremediation of U(VI) contaminated mine water

Oligo-Miocene magnetostratigraphy and rock magnetism of the Xishuigou section, Subei (Gansu Province, western China) and implications for shallow inclinations in central Asia.

Magnetostratigraphy of 222 remanent directions together with late Oligocene to early Miocene mammal and charophyte paleontology suggest that 2179 m of the Xishuigou section (Subei, Gansu Province, China) were deposited from ~26 to ~19 Ma. Stratigraphic patterns of bulk susceptibility, anisotropy of magnetic susceptibility parameters, and natural and anhysteretic remanent magnetization intensities demonstrate that (1) faulting does not significantly affect the record, (2) sediment deposition was relatively continuous, (3) sediment source changed around 23 Ma, and (4) rapid uplift near Subei occurred at 21 Ma. Subei rotated 27° ± 5° counterclockwise with respect to the 20 Ma pole from the Eurasian synthetic apparent polar wander path. Folding and rotation of the section took place after 19 Ma. The paleolatitude of Subei is 14° less than at present and 19° ± 3° less than predicted from the reference pole. Both rock magnetic and paleomagnetic data sets suggest that the unusually low paleolatitude is the result of synsedimentary inclination shallowing, a phenomenon which has likely affected other paleomagnetic data from central Asia

Kex2 protease converts the endoplasmic reticulum α1,2-mannosidase of Candida albicans into a soluble cytosolic form

Cytosolic α-mannosidases are glycosyl hydrolases that participate in the catabolism of cytosolic free N-oligosaccharides. Two soluble α-mannosidases (E-I and E-II) belonging to glycosyl hydrolases family 47 have been described in Candida albicans. We demonstrate that addition of pepstatin A during the preparation of cell homogenates enriched α-mannosidase E-I at the expense of E-II, indicating that the latter is generated by proteolysis during cell disruption. E-I corresponded to a polypeptide of 52 kDa that was associated with mannosidase activity and was recognized by an anti-α1,2-mannosidase antibody. The N-mannan core trimming properties of the purified enzyme E-I were consistent with its classification as a family 47 α1,2-mannosidase. Differential density-gradient centrifugation of homogenates revealed that α1,2-mannosidase E-I was localized to the cytosolic fraction and Golgi-derived vesicles, and that a 65 kDa membrane-bound α1,2-mannosidase was present in endoplasmic reticulum and Golgi-derived vesicles. Distribution of α-mannosidase activity in a kex2Δ null mutant or in wild-type protoplasts treated with monensin demonstrated that the membrane-bound α1,2-mannosidase is processed by Kex2 protease into E-I, recognizing an atypical cleavage site of the precursor. Analysis of cytosolic free N-oligosaccharides revealed that cytosolic α1,2-mannosidase E-I trims free Man8GlcNAc2 isomer B into Man7GlcNAc2 isomer B. This is believed to be the first report demonstrating the presence of soluble α1,2-mannosidase from the glycosyl hydrolases family 47 in a cytosolic compartment of the cell