Fully automatic welding of thick-walled pressure vessels by the narrow gap subarc process

The demands for welding of thick-walled pressure vessels are very stringent. The cost of repairing a weld defect deep down in a weld joint could be very high. As submerged arc welding is considered to be a reliable process for both the welding of pressure vessels and other demanding applications, ESAB chose this process when developing their narrow gap welding technique. This two-pass narrow gap process is described together with the welding and control equipment. The welding results using two types of agglomerated fluxes are presented.     

Disc filtration for separation of flocs from a moving bed bio-film reactor.

A Discfilter with 10 and 18 microm filter openings, respectively, was placed in parallel to a flotation plant for separation of biological flocs from a post-denitrifying Kaldnes Moving Bed Process, the last treatment step at the municipal wastewater treatment plant at Sj?unda, Malm?, Sweden. The effluent concentrations from the 10 and 18 microm filter were 2-5 and 2-8 mg SS L(-1), respectively, which is comparable to, or better than, the flotation plant. Comparison with experiences from activated sludge plants shows that the Discfilter works especially well after the Kaldnes process. Particle size distribution (PSD) studies show that particles larger than the filter openings of 10 and 18 microm are separated with approximately 90% efficiency, whereas most of the smaller particles pass the filter. This fact indicates that the major particle separation mechanism is physical blocking. These findings point to the possibility of improving the prediction of the separation efficiency by combining measurements of turbidity and suspended solids with particle size analysis.     

Cellular UDP-glucose deficiency caused by a single point mutation in the UDP-glucose pyrophosphorylase gene

We previously isolated a mutant cell that is the only mammalian cell reported to have a persistently low level of UDP-glucose. In this work we obtained a spontaneous revertant whose UDP-glucose level lies between those found in the wild type and the mutant cell. The activity of UDP-glucose pyrophosphorylase (UDPG:PP), the enzyme that catalyzes the formation of UDP-glucose, was in the mutant 4% and in the revertant 56% of the activity found in the wild type cell. Sequence analysis of UDPG: PP cDNAs from the mutant cell showed one missense mutation, which changes amino acid residue 115 from glycine to aspartic acid. The substituted glycine is located within the largest stretch of strictly conserved residues among eukaryotic UDPG:PPs. The analysis of the cDNAs from the revertant cell indicated the presence of an equimolar mixture of the wild type and the mutated mRNAs, suggesting that the mutation has reverted in only one of the alleles. In summary, we demonstrate that the G115D substitution in the Chinese hamster UDPG:PP dramatically impairs its enzymatic activity, thereby causing cellular UDP-glucose deficiency.     

Are weaning foods causing impaired iron and zinc status in 1-year-old Swedish infants? A cohort study

Retrobulbar hematoma is a rare complication of blunt periorbital trauma with the potential disastrous consequence of visual impairment and blindness. The preoperative assessment, diagnostic symptoms and signs, as well as the treatment of this condition are reviewed. The patients presented as well as a review of the literature confirm that although retrobulbar hematoma is a rare complication of blunt periorbital trauma, irreversible visual sequelae can be prevented by prompt diagnosis and immediate surgical and pharmacological therapy.     

In vitro kinetics of two human CYP1A1 variant enzymes suggested to be associated with interindividual differences in cancer susceptibility

A genetic polymorphism (A4889-->G) in the human CYP1A1 gene which creates an Ile462-->Val amino acid substitution has been suggested to cause altered enzymatic properties of CYP1A1. Since several epidemiological studies have shown an association between the CYP1A1-Val allele and lung cancer, we considered it of importance to evaluate the in vitro kinetic properties of the two CYP1A1 variants after expression of each cDNA in yeast. No differences were found in K(m) or Vmax for CYP1A1 dependent O-dealkylation of ethoxyresorufin and 3-hydroxylation of benzo(a)pyrene between the two variants. The data indicate that the Ile/Val polymorphism in human CYP1A1 is not functionally important.     

Conformational stability of factor VIIa: biophysical studies of thermal and guanidine hydrochloride-induced denaturation

The binding of the multidomain protein factor VIIa (fVIIa) to tissue factor provides the interprotein communication necessary to make fVIIa an efficient catalyst of the initial event in the extrinsic pathway of blood coagulation. We have investigated the stability of individual domains in fVIIa and the influence of Ca2+ and an irreversible active-site inhibitor (FFR-chloromethyl ketone). Equilibrium guanidine hydrochloride (GuHCl)-induced unfolding monitored by tryptophan fluorescence and far-UV circular dichroism (CD) demonstrated that the gamma-carboxyglutamic acid (Gla) domain unfolds at 0.3 M GuHCl and the serine protease (SP) domain at 3 M GuHCl and that Ca2+ is a prerequisite for the formation of an ordered, compact structure in the Gla domain. The loss of amidolytic activity coincides with the first transition, which is stabilized by the active-site inhibitor, and a change in the environment of the active site is demonstrated using a fluorescent inhibitor (DEGR-chloromethyl ketone). Thermal unfolding monitored by differential scanning calorimetry (DSC) reveals that Ca2+ stabilizes the SP domain slightly, increasing the unfolding temperature by 2.7 degrees C. In addition, Ca2+ is required for a large enthalpy change concomitant with unfolding of the Gla domain, and this unfolding enthalpy is only detectable in the presence of the SP domain, indicating some kind of interaction between these domains. Thermal unfolding measured by CD indicates secondary structural changes at the same temperature as the heat absorption in the DSC but only when both the Gla domain and the SP domain are present together with Ca2+ ions. Taken together, these results indicate a Ca2+-dependent interaction between the Gla domain and the SP domain, implying a high degree of flexibility of the domains in free fVIIa. It is also shown that the epidermal growth factor-like domains are stable at elevated temperatures and high GuHCl concentrations. Moreover, already at physiological temperature, subtle structural changes take place which influence the overall shape of fVIIa and are detrimental to its enzymatic activity.