Anti-N-Acetylprocainamide monoclonal antibody, clone J61X61

The moment magnitude scale (Mw) 6.0 South Napa earthquake caused damage to stainless steel cylindrical tanks used for wine storage and fermentation. The damage observed to the tanks included local buckling of the tank walls, anchorage failure, and damage at the top of the tanks as a result of the catwalk system. Inspections of these tanks after the South Napa earthquake provided the motivation and the basis for investigating the seismic behavior of stainless steel cylindrical tanks used for liquid storage. This investigation focused on (1) the behavior of stainless steel cylindrical tanks in previous earthquakes around the world, and (2) research performed to mitigate this damage. The damage to cylindrical steel tanks after the South Napa earthquake was found to be identical to damage documented by postearthquake reconnaissance reports from around the world. Large-scale experimental research (by other researchers) has already demonstrated the inadequacy of cylindrical tank anchorage details for the seismic risk at winery locations. Simplified elastic models developed by engineers are generally inadequate for predicting the level of stresses and seismic damage (such as local buckling) in cylindrical tanks. This paper summarizes the damage observed after earthquakes to cylindrical steel tanks used in the wine industry, and previous research performed to help mitigate the damage. The authors suggest avenues for future research and code regulation of these tanks to improve seismic performance and reduce the level of risk to wine owners. (C) 2016 American Society of Civil Engineers.

Much of the research on Na+/H+ exchange has been done in prokaryotic models, mainly on the NhaA Na+/H+-exchanger from Escherichia coli (EcNhaA). Two conserved aspartate residues, Asp-163 and Asp-164, are essential for transport and are candidates for possible binding sites for the two H+ that are exchanged for one Na+ to make the overall transport process electrogenic. More recently, a proposed mechanism of transport for EcNhaA has suggested direct binding of one of the transported H+ to the conserved Lys-300 residue, a salt bridge partner of Asp-163. This contention is supported by a study reporting that substitution of the equivalent residue, Lys-305, of a related Na+/H+ antiporter, NapA from Thermus thermophilus, renders the transporter electroneutral. In this work, we sought to establish whether the Lys-300 residue and its partner Asp-163 are essential for the electrogenicity of EcNhaA. To that end, we replaced Lys-300 with Gln, either alone or together with the simultaneous substitution of Asp-163 with Asn, and characterized these transporter variants in electrophysiological experiments combined with H+ transport measurements and stability analysis. We found that K300Q EcNhaA can still support electrogenic Na+/H+ antiport in EcNhaA, but has reduced thermal stability. A parallel electrophysiological investigation of the K305Q variant of TtNapA revealed that it is also electrogenic. Furthermore, replacement of both salt bridge partners in the ion-binding site of EcNhaA produced an electrogenic variant (D163N/K300Q). Our findings indicate that alternative mechanisms sustain EcNhaA activity in the absence of canonical ion-binding residues and that the conserved lysines confer structural stability.